Systems and methods for recognizing or analyzing amino acids, peptides, polypeptides, or proteins

Abstract

Disclosed herein are compositions, methods and kits used in a process for detecting, identifying and characterizing any proteome, protein, peptide and polypeptide molecule and the underlying amino acid sequence. The development of the Conversome™ molecule, for use in any of these processes, comprises a Ligamer element which binds to its accessible, cognate amino acid on a target protein or mixture of proteins and the Ligamer element is conjugated to a specific nucleic acid sequence within a Decodon element corresponding to the cognate amino acid recognized by the Ligamer element. The binding of a mixture of a plurality of unique, specific Conversome molecules to each Conversome's specific cognate amino acid produces a pDNA or pRNA sequence strand matching the translation of the protein'(s) genetic code.

Description

SYSTEMS AND METHODS FOR RECOGNIZING OR ANALYZING AMINO ACIDS, PEPTIDES, POLYPEPTIDES, OR PROTEINSCROSS-REFERENCE

[0001] The present application claims priority to U.S. Provisional Patent Application No. 63 / 741,003, filed on December 31, 2024, entitled “RECOGNIZING AMINO ACIDS, AND USING THESE TO ANALYZE PROTEINS, COMPONENTS, METHODS AND USES,” which is incorporated herein by reference in its entirety for all purposes.FIELD

[0002] The present teachings relate to compositions, methods of producing and using the compositions, and kits to derive nucleic acid sequences that encode amino acids, peptides, polypeptides, or proteins and ways to use the nucleic acid sequences for amino acid, peptide, polypeptide, tor protein detection, identification, three-dimensional (3D) structural identification, or analyses efficiently, expeditiously, or economically.SEQUENCE LISTING

[0003] The instant application contains a Sequence Listing which has been submitted herewith and is hereby incorporated by reference in its entirety. Said .xml copy, created on December 26, 2025, is named PF039243001WQ1, and is 55,161 bytes in size.BACKGROUND

[0004] Proteins constitute, among other things, enzymes and many of the structural elements within a cell. Detection and quantitation of proteins has been hampered by technology which has not improved in decades. Most of these techniques require large amounts of proteins, expensive equipment, or reagents which are expensive, difficult to develop and are specific for each protein. Scientists have long used ribonucleic acid (RNA) as a surrogate for protein analysis, however, it is generally accepted that RNA levels and profiles do not necessarily reflect protein levels and profiles. A method to convert all proteins within a cell, irrespective of sequence and amount, into a format that could be detected and quantified is the “holy grail” of protein analysis.

[0005] The analysis of RNA routinely begins with its conversion en masse into deoxyribonucleic acid (DNA) using reverse transcriptase enzymes (i.e., RNA sequences are converted into corresponding complementary DNA (cDNA) sequences). DNA can then be amplified using DNA polymerases, or detected and quantitated by methods such aspolymerase chain reaction (PCR), quantitative PCR (qPCR) or Next Generation Sequencing (NGS) techniques. No such method for turning some or all proteins within a sample into a stable and detectable format exists. One method currently used for protein detection and quantitation uses mass spectrometers; however, this method requires a great deal of sample, limiting the number of proteins that can be analyzed. Additionally, it requires the use of expensive equipment and highly trained operators. Another set of methods utilize affinity reagents (i.e. , antibodies and aptamers) which are designed to specific “antigenic” sequences. Affinity reagents facilitate and are the basis behind detection methods such as enzyme-linked immunosorbent assay (ELISA), proximity ligation assay (PLA), and Western Blotting, among others. Affinity reagents, such as antibodies, require a large investment in time and money, and their production is costly and can produce inconsistent products. Other affinity reagents do not provide the specificity and affinity needed for most of these detection methods. Most importantly, affinity reagents specifically recognize “antigenic” sites in the protein. However, proteins are not always in the correct conformation and so inaccessible for recognition and binding.

[0006] Affinity reagents can target an amino- or carboxyl-terminal end’s amino acid and create a DNA chain representing the protein sequence (US20190145982A1; Encodia) or use the affinity reagents to carry a molecule that can be detected using an instrument (US20200209257A1; Quantum-Si). These amino acids are then removed using an enzyme or chemical allowing recognition of the next terminal amino acid. Limitations for these methods are that only sequential analysis of amino acids is performed, and dedicated and specialized instrumentation is required to wash away reagents which could interfere with subsequent steps.

[0007] Other technologies improve upon affinity reagents such as aptamers (US-6291184-B1; Somalogic), allowing them to be more easily tailored to different proteins. However, these still recognize an “antigenic” portion of the protein and do not evaluate the underlying sequence of the protein undergoing analysis.

[0008] Other technologies improve upon the presentation of proteins such as arrays which allow an increase in the number of proteins that can be analyzed at once (Zhu H et al. (2001) Global analysis of protein activities using proteome chips. Science. 293: 2101). However, these require protein purification in order to make arrays of proteins to be analyzed with dedicated instrumentation.

[0009] Other protein array technologies utilize less specific affinity reagents in order to recognize proteins on an array (US-10473654-B1; Nautilus). Again, these still require specific instrumentation for the preparation and detection of proteins.

[0010] Improvements on existing methods such as mass spectrometry (US-20150346068-A1; Preomics) only incrementally improve sample preparation, and still require expensive instrumentation.

[0011] Currently there is a need to accurately quantitate proteins across a wide dynamic range, concomitantly detect many proteins, detect low levels of proteins, analyze protein modifications, and discover new proteins. However, current technologies fail to address all of these needs, and many of these needs are not addressed at all.Technological solutions to these needs should ideally be simple and accurate and higher throughput.INCORPORATION BY REFERENCE

[0012] All publications, references, patents, and patent applications mentioned in the document are herein incorporated by reference to the same extent as if each individual publication, reference, patent, or patent application was specifically and individually indicated to be incorporated by reference. In the event of inconsistent usages between this document and those documents so incorporated by reference, the usage in the incorporated reference should be considered supplementary to that of this document; for irreconcilable inconsistencies, the usage in this document controls.

[0013] Reference will now be made in detail to certain claims of the invention, examples of which are illustrated in the accompanying drawings. While the invention will be described in conjunction with the enumerated claims, it will be understood that they are not intended to limit those claims. On the contrary, the invention is intended to cover all alternatives, modifications, and equivalents, which can be included within the scope of the invention as defined by the claims.SUMMARY

[0014] The disclosed compositions and processes offer improvements and advantages over currently used compositions and methods for protein analyses. Basically, the disclosed composition facilitates the direct conversion of a protein into a DNA sequence, called a pDNA™ sequence strand, or a RNA sequence, called a pRNA sequence strand. And the pDNA sequence strand finds uses in processes covering a broad range of DNA (or RNA) analysis methodologies and technologies.

[0015] Applicant has developed a novel adapter / recognition molecule, termed a Conversome™ molecule. Conversome molecules are useful for detection and identification of a plurality of amino acids within any one of a peptide, polypeptide, protein and proteome,herein collectively referred to as a “polypeptide molecule”. The Conversome comprises a Ligamer™ element, which is a binding portion of a Conversome that recognizes a residue of an amino acid or a residue within a polypeptide (whether binding is reversible or irreversible); and a Decodon™ element, which provides a nucleic-acid tag (e.g., single- or double-stranded, DNA / RNA / analogs) that can be concatenated and read out as pDNA or pRNA. A linker moiety is an optional component that in the context of a Conversome, may connect the Ligamer (residue-recognition moiety) to the Decodon (residue-labeling moiety) (e.g., using polyethylene glycol (PEG) or photocleavable spacers).

[0016] A mixture of a plurality of Conversome molecules can be utilized for detection and identification of a plurality of amino acids within any “protein molecule(s).” Each Conversome molecule has a Decodon element with a specific amino acid identifying nucleic acid sequence(s), a Decodon nucleic acid strand. The Decodon element may be linked to a Ligamer element having an amino acid recognition portion. The amino acid recognition portion binds to its cognate amino acid residue within one or more amino acid portions of the polypeptide molecule(s) (either unfold or when interacting with another protein).

[0017] In some embodiments, when adjacent or nearby specific Conversome molecules bind to the polypeptide of interest (e.g., a target protein, etc.) via the Ligamer element, the concatenation of each of the bound specific Conversome molecule’s corresponding Decodon strands to spatially aligned Decodon elements in another Conversome molecule can occur. As concatenation proceeds, a growing nucleic acid sequence, akin to e.g., a cDNA product from an RNA template is formed. This will facilitate conversion of the protein molecule’s(s’) amino acid sequence into the pDNA sequence strand.

[0018] Each Conversome molecule’s Decodon and Ligamer elements are specific for one particular amino acid and can bind a corresponding specific amino acid residue anywhere in the polypeptide molecule’s amino acid sequence. Contrary to recent technologies that can only recognize Amino or Carboxyl terminal amino acids the disclosed Conversome molecules are not limited to amino acid position or a section of a peptide such as an antibody. Additionally, recognition of specific amino acids and binding of all amino acids by their cognate Ligamer element can occur at the same time, unlike technologies which can only bind amino acids sequentially and / or iteratively. Thus, the polypeptide (e.g., protein) molecule’s amino acid sequence serves as a template of the polypeptide (e.g., protein) molecule and is preserved and facilitates an archivable rendering of the exact same, corresponding protein molecule via the pDNA or pRNA sequence strand. Moreover, the conversion of a protein into its DNA or RNA sequence is carried out in solution in realtime instead of on a solid surface, and so does not have a lag time for experimental execution and analysis of results versus other protein molecule analysis and sequencing technologies. Consider, for example, that either monoclonal antibodies or protein microarrays must first be created and built, respectively.

[0019] The post-reaction polypeptide molecule sequence strand can serve as a template and may be preserved for future protein analytics, as opposed to being destroyed - rendering the exact same protein molecule(s) “archivable”. By contrast, many other protein analysis technologies require destruction of the sample. For example, analyses of proteins can undergo destruction during Tandem Mass Spectrometry, Edman degradation, or other technologies which use aminopeptidases.

[0020] Two or more of any of the Conversome molecules (from a pool of a mixture of a plurality of Conversome molecules) can become linked together, via concatenation by their Decodon elements’ oligonucleotide nucleic acid sequences, in an order based on the sequence of the amino acids in the protein molecule’s amino acid sequence. And the number of amino acid recognition reagents are not restricted or limited in number. In other words, all known amino acids, regardless if natural / native proteinogenic, non-proteinogenic, modified and synthetic amino acids in origin, are associated with just one Decodon element sequence and a corresponding Ligamer element recognition portion. The result is that the Conversome molecules can be utilized for broad and extensive protein analysis applications regardless of origin of a protein molecule’s(s’) sample source or taxonomic classification.

[0021] Unique to the claimed innovation is that one does not need to know the protein sequence in question in order to detect it because a plurality of Conversome molecules (recognizing many different amino acids) in a composition can represent the proteinogenic amino acids and as many non-proteinogenic, modified or synthetic amino acids as one wishes to create for a specific Conversome molecule. The use of Conversome molecules can be considered to be similar to how you don’t need to know the DNA sequence to amplify it (except for the primers) because all of the nucleotides needed for amplification are present in the reaction. Thus, the use of Conversome molecules can be likened to whole genome sequencing.

[0022] Pre-linking two or more Conversome molecules, each with double-stranded DNA Decodons within each Conversome’s Decodon element, forms pre-linked OligoConversome™ molecules. At least two, three, four, five, six, seven, eight, nine, ten, or another suitable number of Conversome molecules can be pre-linked to form OligoConversome molecules. The time needed to generate reagents (OligoConversome molecules) in order to quantitate one protein is typically very short. This is similar to howfast oligo synthesis is because Conversome molecules are available for all amino acids, natural, proteinogenic, modified, non-proteinogenic, and synthetic amino acids. Knowing a protein molecule of interest’s amino acid sequence can be beneficial for the assembly of OligoConversomes to detect and / or quantitate the protein molecule of interest.

[0023] OligoConversome molecules (an OligoConversome) can be made on demand, similar to oligo synthesis - which can be used for producing protein specific affinity reagents. However, unlike antibodies, which require additional time for immunization and creating a monoclonal antibody, the OligoConversome molecules can be synthesized in about two days with current techniques.

[0024] The Conversome molecule can be used to detect / identify amino acids and amino acid sequences within any one or more of: a target polypeptide, protein mixture and / or to distinguish one or more protein(s) from another as well as numerous other protein analyses methods listed infra.

[0025] In practice of the claimed invention each Decodon element’s “Decodon strand sequence” represents one amino acid. And, the Decodon element’s nucleic acid sequence is specific for just the one amino acid, regardless of the protein’s source including, but not limited to, a bacteria, virus, mycoplasm, organelle, cell, tissue, organ, Kingdom, phylum, class, order, family, genus, and species or genetic code.

[0026] The current disclosure addresses the need in the art for easily converting all proteins within a cell, bodily fluid sample, tissue, biopsy, organ biopsy, proteome, environmental sample, bacterial sample, 3-D printed sample, irrespective of sequence and amount, into a format that could be detected and quantified. This can be through converting an entire proteome into DNA (or RNA) sequences for use in quantitation and identification of protein sequences from each protein’s corresponding DNA / RNA sequence. This can be accomplished through construction of amino acid specific adapter / recognition molecules to identify each of the amino acids, in the order they exist, within the proteome, protein, peptide or polypeptide sequence analyzed. Decodon strands, when assembled in the correct order, can be used to determine the amino acid sequence ofa target protein.

[0027] The resulting pDNA or pRNA nucleic acid sequence(s) representing a protein('s) amino acid sequence(s) can be analyzable by numerous applications and technologies including, but not limited to, methods of protein: detection, quantitation, identification, discovery, discovering new protein modification positions, and quantitate the amount and type of protein modifications via qPCR, Next Generation Sequencing (NGS), digital PCR, Sanger Sequencing and other methods for protein analyses as is known to the skilled artisan.

[0028] These and other features, aspects, and advantages of the present invention will become better understood with reference to the following description and claims.BRIEF DESCRIPTION OF THE DRAWINGS

[0029] These and other features, aspects, and advantages of the present invention will become better understood with regard to the following description, appended claims, and accompanying drawings (referred to as “Figures” or “FIGs.”):

[0030] Figure 1 illustrates a Conversome molecule consisting of amino acid binding element second end-linker-nucleic acid oligonucleotide opposite first end:

[0031] Figure 1A depicts a Conversome™ molecule (100) consisting of a Ligamer™ element (101) having an amino acid recognition portion (102), a Linker element (108) connecting the Ligamer element to a Decodon element (103) having a DNA (or RNA) nucleic acid sequence specific for an amino acid. In this example, the Decodon DNA nucleic acid is a single strand cis-Decodon strand (104).

[0032] Figure 1 B depicts the Conversome molecule (110) similar to that of FIG. 1 A with a double-stranded Decodon element (106) with complementary DNA nucleic acid sequences.

[0033] Figure 2 (SEQ ID Nos: 41-42) illustrates the disclosed innovation as a method for using pDNA (or pRNA) to detect a protein molecule.

[0034] Figure 2A depicts, in a sample, one of a plurality of unfolded polypeptide sequences (201) following denaturation of at least one specific protein (200) within a mixture of proteins to be detected.

[0035] Figure 2B illustrates the addition of a plurality of different, specific Conversome molecules each comprising at a first end a specific Decodon double-stranded DNA nucleic acid sequence connected by a linker to the opposite end of the Conversome molecule, which is a second end, with a corresponding, specific, Ligamer element which has a cognate / reciprocal amino acid binding molecule (e.g., (110)) in a solution of the unfolded polypeptide sequence(s) of FIG. 2A. Each Conversome molecule will bind to its corresponding cognate / reciprocal amino acid within the unfolded polypeptide sequences(s).

[0036] Figure 2C-2F illustrates binding of the plurality of different, specific Conversome molecules and the addition of a concatenation agent to concatenate the Decodon element’s double-stranded DNA nucleic acid sequences by a ligase or other method creating a pDNA sequence strand.

[0037] Figures 2D, 2E and 2F illustrate the concatenation of one strand of the specific Decodon double-stranded DNA nucleic acid sequences of FIG. 20.

[0038] Figure 2G depicts denaturation of the concatenated DNA strands releasing the concatenated DNA sequence from the Decodon double-stranded DNA nucleic acid sequences and enabling detection of the concatenated DNA sequence derived from the target protein.

[0039] Figure 3A (SEQ ID Nos: 41-42) illustrates concatenation of both DNA strands as illustrated in FIG. 2C.

[0040] Figure 3B (SEQ ID NO: 41) illustrates concatenation of specific Conversomes having a single-stranded DNA or RNA Decodons.

[0041] Figure 3C (SEQ ID Nos: 41-42) depicts degradation of the linkers joining the Decodon to their Ligamer thereby releasing the concatenated pDNA to be detected.

[0042] Figure 3D (SEQ ID NO: 42) depicts an RNA cis-Decodon which is subsequently degraded with a nuclease or with heating and divalent cation to release the pDNA for detection.

[0043] Figure 3E (SEQ ID Nos: 41-42) depicts chemical concatenation of Decodons.

[0044] Figure 4 (SEQ ID Nos: 43-44) depicts a form of targeted conversion of a targeted protein.

[0045] Figure 4A depicts addition of a pair of pre-linked Conversomes (412 and 413) called OligoConversomes with double-stranded DNA called OligoDecodons (pre-linked oligonucleotide nucleic acid sequences, 402 and 403) to a solution containing the denatured protein (401).

[0046] Figure 4B illustrates the binding of each pre-linked OligoConversome from FIG. 4A to its specific reciprocal amino acids within the denatured protein’s sequence (i.e. , a sequence of amino acids).

[0047] Figure 4C illustrates concatenation of the pre-linked OligoConversomes’ double-stranded DNA OligoDecodon oligonucleotide nucleic acid sequences (concatenation of the trans-Decodon sequences) from FIGS. 4A-4B into a single oligonucleotide nucleic acid sequence, the OligoDecodon pDNA sequence (420).

[0048] Figure 4D depicts release and detection from FIG. 4C of the single oligonucleotide nucleic acid sequence (430) the OligoDecodon pDNA.

[0049] Figure 5 (SEQ ID Nos: 45-48) illustrates the use of a Conversome molecule(s) having a non-specific affinity to fill in gaps between bound specificConversome molecules. Often knowing the position and identify of three to 10 or more amino acids within a protein sequence can be adequate for protein sequence identification and / or detection.

[0050] Figure 5A depicts addition of specific Conversomes (216, 213, 212) for a subset of amino acids present in the target, denatured protein in solution.

[0051] Figure 5B depicts binding of the specific Conversomes to their cognate amino acids, leaving gaps of unbound amino acids between the bound subset of amino acids. The unbound Conversomes can then be washed after binding of the specific Conversome molecules.

[0052] Figure 5C illustrates the further addition of non-specific Conversome molecule capable of non-specifically binding to all amino acids.

[0053] Figure 5D shows “filling in” of gaps by binding of non-specific Conversome molecules. The unbound Conversomes are then washed after binding of the nonspecific amino acid recognition portion.

[0054] Figure 5E illustrates the concatenation of the bound Conversomes by a ligase or other method creating a pDNA sequence strand.

[0055] Figure 6 (SEQ ID Nos: 49-50) illustrates a DNA detection method using qPCR (singleplex or multiplex, probe or intercalation based).

[0056] Figure 6A depicts an unfolded protein (401).

[0057] Figure 6B illustrates the addition of a mixture of (a plurality of) specific Conversome molecules.

[0058] Figure 6C illustrates the binding of a mixture of specific Conversome molecules to each specific Conversome’s cognate amino acid.

[0059] Figure 6D illustrates concatenation of trans-Decodon strands and cisDecodons.

[0060] Figure 6E illustrates release of the concatenated pDNA strand and binding of two primers and a probe to the pDNA strand for qPCR by 5’ nuclease.

[0061] Figure 6F shows the initiation of qPCR by 5’ nuclease to the released pDNA (670).

[0062] Figure 6G depicts addition of two primers for intercalation based qPCRs (continued from 6D).

[0063] Figure 6H shows qPCR with an intercalating dye on the pDNA sequence strand (670).

[0064] Figure 7 (SEQ ID Nos: 49-50) illustrates Targeted NGS by the addition of sets of primers (panel of primers); 700), following converting the entire proteome to pDNA and a subset of protein sequences are amplified by PGR.

[0065] Figure 8 (SEQ ID Nos: 49-50) illustrates release of pDNA sequence strand(s) and attachment of DNA Adapters to every pDNA sequence to convert the pDNA sequence strands into library molecules for analysis by NGS.

[0066] Figure 9 illustrates detection of a known, specific protein sequence(s) using OligoConversomes.

[0067] Figure 9A depicts the use of OligoConversomes (900) pre-linked together based on the known sequence of the protein to be detected and having a Detection molecule (901) attached at the 5’ end of the pre-linked Decodon strands. The Detection molecule could be a fluor or enzyme, a bead with different density, or a magnetic bead (or other affinity reagent).

[0068] Figure 9B illustrates detection of a specific protein sequence following binding of the linked Conversomes and the protein sequence is detected.

[0069] Figure 10 illustrates pseudo-Conversomes pre-linked Ligamers for detection of specific amino acid sequences in a target protein. Single-stranded nucleic acids or other types of chemical linkages (1000) are attached and connecting each Linker element to its Ligamer element and pre-link each of a first end of two or more Linker elements whose opposite, second ends are each attached to two or more Ligamer amino acid recognition portions creating pre-linked Ligamer elements. Addition of the pre-linked Ligamer elements to the solution containing a target protein allow the pre-linked Ligamers’ recognition portions to bind to their comparably positioned reciprocal (cognate) amino acids within the target protein. Detecting the protein sequence can then be done via the pre-linked Ligamers (1000) which are connected to a fluorescent molecule or via an enriched immunoprecipitation assay via a linked bead ((901) FIG. 10)

[0070] Figure 11 (SEQ ID NO: 51) illustrates how a protein molecule’s sequence is detected without pre-linking specific Conversome molecules.

[0071] Figure 11 A depicts addition of a mixture of a plurality of specific Conversome molecules (1100, 1110,1120, 1130, 1140, 1150).

[0072] Figure 11 B depicts binding of each specific Conversome molecule to its cognate / reciprocal amino acid along a defined conformation, target polypeptide in a solution.

[0073] Figure 11C depicts addition and binding of a labeled Detection molecule (901), complementary, oligonucleotide nucleic acid sequence (1170) that targets / recognizes specific cis-Decodon strands’ oligonucleotide nucleic acid sequences within the target protein’s amino acid sequence. Unbound oligo is washed away.

[0074] Figure 11 D depicts detection of the target protein via at least one of a fluor, enzyme, enriched via immunoprecipitation, or captured if a magnetic bead is attached to the complementary oligonucleotide sequence.

[0075] Figure 12 (SEQ ID Nos: 52-53) illustrates a method for detection of protein secondary and tertiary structures.

[0076] Figure 12A depicts the addition of Conversomes to an intact protein (200) in its natural state. When proteins are folded in the native state there are some amino acids that are accessible (e.g., 202, 206, 205, 204).

[0077] Figure 12B depicts the Conversomes (212, 216, 215, 214). binding to accessible, cognate amino acids (202, 206, 205, 204) on the intact protein in its natural state as shown in FIG. 12A.

[0078] Figures 12C and 12D illustrate the concatenation of trans-Decodons which are in an spatial alignment that permits interlocking and concatenation to other bound Conversomes. This creates a “pattern” based on the Conversomes that are spatially aligned to each other. Monitoring the protein’s secondary and tertiary structures can result in changes in the “pattern” as changes in structure will change which Conversomes can concatenate to one another.

[0079] Figure 12E illustrates the concatenation of bound Conversomes’ transDecodon double-stranded DNA nucleic acid sequences (1200) in a spatial alignment that permits interlocking and concatenation to other bound Conversomes’ trans-Decodon double-stranded DNA nucleic acid sequences following their concatenation.

[0080] Figure 12F illustrates the denaturation of the pDNA (concatenated trans-Decodon strands released from the cis-Decodon strands DNA (1210) and detection of the concatenated nucleic acid can be by NGS, qPCR or using a fluor or enzyme, or enriched via immunoprecipitation, or captured if a magnetic bead (e.g., (901)) or other amino acid recognition portion) is a attached to the pDNA sequence strand (not shown).

[0081] Figure 13 (SEQ ID Nos: 52-53) illustrates a method for detection of protein quaternary structure and protein:protein interactions.

[0082] Figure 13A depicts the addition of Conversomes to intact proteins (1300 and 1310) which are interacting in their natural state. When proteins are folded in the native state there are some amino acids that are accessible.

[0083] Figure 13B depicts the Conversomes binding to accessible, cognate amino acids on the intact proteins in their natural state as shown in FIG. 13A.

[0084] Figures 13C and 13D illustrate the concatenation of trans-Decodons which are in an spatial alignment that permits interlocking and concatenation to other bound Conversomes.

[0085] Figure 13E illustrates the concatenated bound Conversomes’ trans-Decodon double-stranded DNA nucleic acid sequences (1200) in an spatial alignment that permits interlocking and concatenation to other bound Conversomes’ trans-Decodon doublestranded DNA nucleic acid sequences. Following their concatenation a “pattern” based on the Conversomes that are close to each other can be established. Monitoring the proteins’ structures and interactions can result in changes in the “pattern” as changes in structure will change which Conversomes can concatenate to one another.

[0086] Figure 13F illustrates the denaturation of the pDNA (concatenated transstrands) and its release (1210) from the bound Conversome molecules. The pDNA (1210) can be analyzed by NGS, qPCR or using a fluor or enzyme, or enriched via immunoprecipitation, or captured if a magnetic bead (or other affinity reagent) that is attached to the pDNA to detect and, or quantify protein:protein interactions.

[0087] Figure 14 (SEQ ID Nos: 49-50 and 54-55) describes the detection of modified amino acids.

[0088] Figure 14A depicts two proteins (1401 and 1404) from the same polypeptide sequence; however, protein (1404) has a modification at one of the amino acids (1410) compared to the same position for the same amino acid (1400).

[0089] Figure 14B illustrates the addition of a mixture of a plurality of different, specific Conversome molecules. One of these Conversomes (212) recognizes the natural amino acid (1400), and a second different, specific Conversome (1414) with a different Decodon strand sequence recognizes the modified amino acid (1410).

[0090] Figure 14C shows the Conversomes binding to their cognate amino acids.

[0091] Figure 14D illustrates the concatenation of the cis- and trans-Decodon double-stranded DNA nucleic acid sequences by a ligase or other method creating a pDNA sequence strand, or a nucleotide polymer from an amino acid polymer.

[0092] Figure 14E illustrates the denaturation of the pDNA (1420 and 1430) and detection and / or analysis of the concatenated nucleic acid by NGS, qPCR or using a fluor, enzyme, enriched via immunoprecipitation. Of note is that the two pDNA sequence strands are mostly the same except for one portion of the sequence, where one sequence represents the natural, unmodified amino acid (1420) and the other sequence represents the modified amino acid (1430) - resulting from binding by a different, specific Conversome with a different amino acid recognition portion and specific Decodon sequence strand

[0093] Figure 15 illustrates Decodon strand variations to provide orientation, direction concatenation availability and various over-hanging ends.

[0094] Figure 15A illustrates different Decodon types with 0, 1 , 2, 3 or more 5’ or 3’ overhangs. Decodons strands can be polymeric, comprising 2 to more than 300 nucleic acids in length.

[0095] Decodon ends can also have, either alone or in addition to overhanging ends, ends with one or more of a OH, PO4, H, or blocked (Detection molecule(s) (901). Figure 15B demonstrates modifications to the Decodon strand’s ends which can limit the orientation of concatenation by either blocking (901) or not providing an active moiety on one, both or the other end of the Decodon strand.

[0096] Figure 15C illustrates a Detection Molecule (a block (901)) on one end of the Decodon strand, blocking the end from concatenation. An H on one end of the Decodon strand also leaves only the opposite end with either an OH or PO4 available to concatenate (not shown).

[0097] Figure 15D illustrates the presence of Hydrogen (H) on complementary ends of double-stranded Decodon strands, leaving the opposite ends of the complementary strands available to concatenate.

[0098] Figure 15E illustrates all four ends of double-stranded Decodon strands available to concatenate. The presence of OH and PO4 (active moieties) on both doublestranded Decodon strands’ ends allows for concatenation.

[0099] Figure 15F illustrates the presence of Hydrogen (H) on both ends, of one strand of double-stranded Decodon strands, being blocked from concatenating. The presence in the other complementary, double-stranded Decodon strand of OH and PO4 at the ends indicates that the other complementary strand will be available to concatenate.[000100] Figure 16A illustrates the disclosed innovation as a method for using a single Conversome molecule to detect two or more, specific amino acids (1600 and 1601) on the same polypeptide strand. The single Ligamer element has been modified to have two, different, cognate amino acid recognition / binding portions ((1602) and (1604), respectively) linked to one Decodon element having a single, specific oligonucleotide nucleic acid sequence ((1606) and (1608, respectively) representing each Ligamer element’s two amino acid recognition / binding portions ((1602) and (1604)), respectively.[000101] Figure 16B illustrates two specific Conversome molecules (1600) and (1601) Ligamer elements with their respective two different, cognate amino acid recognition / binding portions (1602 and 1604) each bound to the two different corresponding reciprocal amino acids (two cognate, adjacent amino acids for each of the two different, cognate amino acid recognition / binding portions (1602 and 1604) within the unfolded polypeptide sequences(s) (401).[000102] Figure 16C illustrates addition of a ligase (230) or another concatenation reagent.[000103] Figures 16D and 16E illustrate the concatenation of the trans-Decodon strands of each of the two specific Conversomes of FIG. 16C to create a pDNA sequence strand (1618).[000104] Figure 16F depicts denaturation of the concatenated pDNA sequencing strand (1620) enabling detection of the concatenated pDNA sequence strand (1620) derived from the target protein.[000105] Figure 17 graphically illustrates data analysis of protein isoforms by quantification of isoforms in a normal versus diseased state(s). The Conversome molecules can be used to identify protein expression patterns in a patient before, during and possibly after therapeutic intervention; they can also provide therapeutic efficacy, suggest duration of treatment and institution of a remission, disease staging, and / or a reoccurrence ahead of a patient presenting symptoms.[000106] Figure 18 illustrates 50 patients’ Proteome analysis. Next Generation Sequencing of pDNA sequencing strands from a plurality of selected proteins is prepared from each patient and data will be visualized as clusters of similar proteome profiles using something such as Uniform Manifold Approximation and Projection (UMAP). The Conversome molecules can be used to identify protein expression patterns in a patient population but will provide predictive analytics of both immediate, interim, and long-term disease conditions, risks and projections.[000107] Figure 19 (SEQ ID NO: 51) illustrates the disclosed innovation using illustrated targeted Conversome molecules’ cis-Decodon strands nucleic acid sequences, not pre-linked, for detection of specific target protein(s) sequences.[000108] Figure 19A illustrates the addition of Conversome molecules (1100, 1110, 1120, 1130, 1140, and 1150) with cis-Decodon strands to a protein sample (401).[000109] Figure 19B illustrates binding of the Conversomes to their cognate amino acids.[000110] Figure 19C illustrates addition of a splint oligonucleotide (1900).[000111] Figure 19D illustrates binding of the splint oligonucleotide (1902) to its cognate sequence.[000112] Figures 19E to 19G illustrate addition of a concatenation agent (230) and concatenation of the cis-Decodon strands which are bound by the splint oligo.[000113] Figure 19H illustrates the splint oligonucleotide bound to the concatenated cis-Decodons (1904).[000114] Figure 191 illustrates denaturation and release of the pDNA sequence strand. (1906).[000115] Figure 20A (SEQ ID Nos: 8-9 and 56) illustrates assembly of Conversomes via click chemistry.[000116] Figure 20B illustrates construction examples of monospecific (multi-amino acid) Conversomes (i.e., OligoConversomes).[000117] FIG. 20C provides experimental data of assembling Conversomes under different conditions.[000118] Figure 20D provides experimental data depicting high performance liquid chromatography (HPLC) resolution of Conversome assembly Intermediates.[000119] Figure 20E provides experimental data of denaturing polyacrylamide gel electrophoresis (PAGE) characterization of assembly fractions.[000120] Figure 20F provides experimental data for constructing bispecific Conversomes carrying two Ligamers recognizing different amino acids and a single Decodon, purified and similarly evaluated via denaturing PAGE and HPLC.[000121] Figure 21A illustrates ligation-based Conversion workflow for qPCR readout.[000122] Figure 21 B illustrates an exemplary assay workflow for qPCR detection and library prep compatibility.[000123] Figure 22A (SEQ ID Nos: 10-11 and 58) provides experimental data where pDNA signal is peptide dependent.[000124] Figure 22B (SEQ ID Nos: 11-12 and 60-61) provides experimental data of peptides with tri-nucleotide sequences and detection signal over background.[000125] Figure 22C (SEQ ID Nos: 12-13 and 57) illustrates exemplary peptidedependent full-length pDNA readouts for SSRRWW (SEQ ID NO: 12) peptides. Including examples of unique molecular barcodes integration in pDNA.[000126] Figure 22D (SEQ ID NO: 12) provides experimental data that full-length pDNA mapping occurred at significantly higher frequency in the peptide-dependent reaction (21.6%) than in trans-Decodon only (6.7%) and peptide-independent supernatant (8.5%[000127] Figure 22E (SEQ ID Nos: 14-36) illustrates targeted “Pep-Pipe” OligoConversome Design for ESR1.[000128] Figure 23A illustrates a schematic for short interlocking spatial alignment extension hybridization “LAX” domains flanking Decodon tags.[000129] Figure 23B continues to expand on the schematic of FIG. 23A, and illustrates complementary trans-Decodons with LAX domains.[000130] Figure 23C continues to expand on the schematic of FIGs. 23A-B, and illustrates extension of trans-joined Decodons.[000131] Figure 23D illustrates the product of expansion of steps FIGs. 23A-C.[000132] Figure 24 A-B (SEQ ID Nos: 11 , 37-40 and 59) provides experimental data on the Conversome mediated enrichment of targeted peptides containing arginine in a mixed background. Demonstrated that Conversome mediated affinity-based capture can enrich target peptides in a background of mixtures with high purity.DETAILED DESCRIPTION OF VARIOUS EMBODIMENTS[000133] Before the present compositions and methods are described, it is to be understood that this invention is not limited to particular compositions, methods, and experimental conditions described, as such compositions, methods, and conditions may vary. It is also to be understood that the terminology used herein is for purposes of describing particular embodiments only, and is not intended to be limiting.[000134] DEFINITIONS[000135] Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. As used herein, the recited terms have the following meanings. The following definitions are included to provide a clear and consistent understanding of the specification and claims. Any methods and materials similar or equivalent to those described herein can be used in the practice or testing of the disclosed invention, as it will be understood that modifications and variations are encompassed within the spirit and scope of the instant disclosure.[000136] References in the specification to "one embodiment," "an embodiment," "another embodiment," and the like, indicate that the described embodiment can include a particular aspect, feature, structure, moiety, or characteristic, but every embodiment may not necessarily include the particular aspect, feature, structure, moiety, or characteristic. Moreover, such phrases are not necessarily referring to the same embodiment. Further, when a particular aspect, feature, structure, moiety, or characteristic is described in connection with an embodiment, it is submitted that it is within the knowledge of one of ordinary skill in the art to effect or connect such aspect, feature, structure, moiety, or characteristic in connection with other embodiments whether or not explicitly described.[000137] It is further noted that the claims may be drafted to exclude an optional element. As such, this statement is intended to serve as antecedent basis for the use of exclusive terminology, such as "solely," "only," "other than", and the like, in connection with any element described herein, and / or the recitation of claim elements or use of "negative" limitations.[000138] The term "and / or" means any one of the items, any combination of the items, or all of the items with which this term is associated. The phrases "one or more" and "at least one" when read in context of its usage are readily understood by one of skill in the art, particularly. For example, the phrase can mean one, two, three, four, five, six, ten, 100, or any upper limit approximately 10, 100, or 1000 times higher than a recited lower limit.[000139] As will be understood by one skilled in the art, for any and all purposes, particularly in terms of providing a written description, all ranges recited herein also encompass any and all possible sub-ranges and combinations of sub-ranges thereof, as well as the individual values making up the range, particularly integer values. A recited range (e.g., weight percentages or carbon groups) includes each specific value, integer, decimal, or identity within the range as if each numerical value and sub-range is explicitly recited. As a non-limiting example, each range discussed herein can be readily broken down into a lower third, middle third and upper third, as well as nested ranges within alarger range, etc. As will also be understood by one skilled in the art, all language such as "up to", "at least", "greater than", "less than", "more than", "or more", and the like, include the number recited and such terms refer to ranges that can be subsequently broken down into sub-ranges.[000140] For example, a range of "about 1 % to about 5%" or "about 0.1 % to 5%" should be interpreted to include not just about 1% to about 5%, but also the individual values (e.g., 1%, 2%, 3%, and 4%) and the sub-ranges (e.g., 0.1% to 0.5%, 1.1% to 2.2%, 3.3% to 4.4%) within the indicated range. The term "about" as used herein can allow for a degree of variability in a value or range, for example, within 10%, within 5%, or within 1% of a stated value or of a stated limit of a range. For example, "about 50" percent can in some embodiments carry a variation from 45 to 55 percent. In yet another example, “about 10.0 wt.%” can be between 9.5 wt.% and 10.5 wt.%.[000141] One skilled in the art will also readily recognize that where members are grouped together in a common manner, such as in a Markush group, the invention encompasses not only the entire group listed as a whole, but each member of the group individually and all possible subgroups of the main group. Additionally, for all purposes, the invention encompasses not only the main group, but also the main group absent one or more of the group members. The invention therefore envisages the explicit exclusion of any one or more of members of a recited group. Accordingly, provisos may apply to any of the disclosed categories or embodiments whereby any one or more of the recited elements, species, or embodiments, may be excluded from such categories or embodiments, for example, for use in an explicit negative limitation.[000142] For integer ranges, the term "about" can include one or two integers greater than and / or less than a recited integer at each end of the range. Unless indicated otherwise herein, the term "about" is intended to include values, e.g., weight percentages, proximate to the recited range that are equivalent in terms of the functionality of the individual ingredient, element, the composition, or the embodiment. The term about can also modify the end-points of a recited range as discuss above in this paragraph.[000143] In this document, the terms "a," "an," or "the" are used to include one or more than one unless the context clearly dictates otherwise. Thus, for example, a reference to "a component" includes a plurality of such components, so that a component Z includes a plurality of components Z. The term "or" is used to refer to a nonexclusive "or" unless otherwise indicated. In addition, it is to be understood that the phraseology or terminology employed herein, and not otherwise defined, is for the purpose of description only and not of limitation. Any use of section headings is intended to aid reading of thedocument and is not to be interpreted as limiting; Information that is relevant to a section heading may occur within or outside of that particular section.[000144] In the methods or processes described herein, the steps can be carried out in any order without departing from the principles of the invention, except when a temporal or operational sequence is explicitly recited.[000145] Furthermore, specified steps can be carried out concurrently unless explicit claim language recites that they be carried out separately. For example, a claimed step of doing A and a claimed step of doing B can be conducted simultaneously within a single operation, and the resulting process will fall within the literal scope of the claimed process. The terms “adjacent amino acids” and “consecutive amino acids” are used interchangeably and refers to two or more amino acids in sequence, next to one another in a sequence of amino acids that encode for a polypeptide, protein and proteome aka “protein molecule.”[000146] The terms “amino acid specific” and “specific amino acid” are used interchangeably and refer to 22 different and specific DNA nucleic acid sequences, e.g., a Decodon strand sequence having a specific trimer to hexamer or more in length of DNA nucleic acids, found in the Decodon region of a Conversome molecule, that can be used to detect or identify and is specific for each of the 22 naturally or artificially occurring amino acids. Additional Decodon nucleic acid sequences are envisioned for specific detection or identification and are specific for modified amino acids, non-naturally occurring amino acids and chemically modified amino acids.[000147] As used herein, “residue” means a monomeric unit of a biomolecule, including: (i) an amino acid residue, i.e., the portion of an amino acid that is present within, or available to be incorporated into, a peptide, polypeptide, or protein; and (ii) a peptide residue, i.e., the portion of a peptide, polypeptide, or protein corresponding to a single amino-acid-derived unit within the polymer chain. A residue includes the backbone and side-chain atoms of the unit as they exist in the relevant chemical context, including at internal positions and at the N- or C-terminus, and irrespective of whether atoms lost or transformed during bond formation (e.g., OH of the carboxyl and / or H of the amine in amide formation) are present in the free monomeric form. For clarity, an “amino acid residue” encompasses natural and non-natural amino acids; enantiomers, diastereomers, isotopologues, and isosteres; and derivatives, including protected forms, mimetics, analogs, homologs, and post-synthetic or post-translationally modified forms (e.g., phosphorylation, glycosylation, methylation, acetylation, lipidation, sulfation, ubiquitination, or nitrosylation), as well as converted or transformed forms arising in situ (e.g., oxidation, reduction, deamidation, cyclization, or crosslinking) and adducts or addition attachments(e.g., conjugation to small molecules, polymers, labels, linkers, tags, or other substituents). A “peptide residue” is the corresponding unit within a peptide, polypeptide, or protein, inclusive of any such modifications, derivatives, conversions, crosslinks, or attachments present in that macromolecular context.[000148] Unless otherwise specified, references to a “residue” include a residue of an amino acid, one or more residues of a peptide, polypeptide, or protein, and their derivatives and modified or converted forms, as well as residues bearing covalent or non-covalent addition attachments, including linkers and nucleic-acid tags. The term encompasses residues that are reversibly or irreversibly recognized or bound by a residue recognition moiety."[000149] The term “detectable unfolded polypeptide sequence “ as used herein represents an unfolded polypeptide sequence identifiable / detectable by the amino acid sequence as determined from each corresponding specific Conversomes’ specific DNA nucleic acids within each Decodon and from the same concatenated together to form a strand specific oligonucleotide sequence (pDNA) representing each unfolded polypeptide sequence(s).[000150] The phrases “residue-recognition moiety”, “amino acid recognition portion,” “amino acid recognition portion,” cognate amino acid binding molecule,” “specific amino acid recognition portion,” “specific amino acid recognition portion,” and “specific, reciprocal amino acid binding molecule” are used interchangeably and as used herein refers to the “Ligamer element’s” molecular end which has high binding propensity and specificity to its specific cognate (reciprocal) amino acid found on the “protein molecule.”[000151] The phrase “cognate amino acid molecule” as used herein refers to the amino acid corresponding to and which may be bound by the “Ligamer element’s” specific amino acid recognition portion (i.e. , residue-recognition moiety) of the Conversome molecule.[000152] The phrase “chemical ligation” as used herein refers to the concatenation of a first “Conversome molecule’s” “Decodon element’s” “oligonucleotide nucleic acid sequence strand(s)” to at least a second Conversome molecule’s Decodon element’s oligonucleotide nucleic acid sequence strand(s) to form an “pDNA strand”. The concatenation can be between two or more “single cis-Decodon strand(s),” two or more trans-Decodon strand(s) and two or more “double Decodon strand(s)”. The double Decodon strand(s) resulting from the pairing of the “cis-Decodon” to its complementary “trans-Decodon strand.” The respective Decodons’ strands are joined by ligation as a result of a “chemical ligation” chemistry selected from the group consisting of amongst others,Click Chemistry, reductive amination, and phosphoramidite chemistry as is known to the skilled artisan.[000153] The terms “concatenate,” “concatenating,” and “concatenation” are used interchangeably and refers to the action of linking things together in a series. The concatenation can be linking two or more Decodon strand’s nucleic acid sequences, such as single cis-Decodon strands, double-stranded Decodon strands, trans-Decodon strands, and two or more Ligamer elements’ with two or more amino acid recognition portions whose Decodon strands are concatenated together as illustrated in Fig. 16E.[000154] The phrases “concatenating agent’ and “concatenation agent” are used interchangeably and refer to agents that may support the concatenation of a first Conversome molecule’s and its Decodon element’s oligonucleotide nucleic acid sequence strand(s)” to at least a second Conversome molecule’s Decodon element’s oligonucleotide nucleic acid sequence strand(s) to form an pDNA strand. The concatenation can be between two or more “single cis-Decodon strand(s),” one or more cis-Decodon strand(s) and one or more “double Decodon strand(s),” and two or more “double Decodon strand(s).” The double Decodon strand(s) resulting from the pairing of the “cis-Decodon” to its complementary “trans-Decodon strand.” The respective Decodons’ strands can be joined by an enzyme selected from the group consisting of: T4 DNA Ligase, RtcB Ligase, T3 DNA Ligase, T7 DNA ligase, E. coli DNA Ligase, SplintR Ligase, TaqDNA Ligase, 9°N DNA Ligase, T4 RNA Ligase 1, T4 RNA Ligase 2, Aminoacyl tRNA synthetase, Succinyl coenzyme A synthetase, Thiokinase, Ubiquitin Ligase, argininosuccinate synthetase, Gamma-glutamyl carboxylase, Polyketide synthase, DNA Ligase, Chelatases, and Glutamate-cysteine ligase, amongst others known to the skilled artisan.[000155] The term “Conversomes” and “Conversome™ molecules” are used interchangeably herein and refer to molecules that can be used for reassembly and direct translation of a “protein molecule’s” amino acid sequence into its oligonucleotide nucleic acid sequence. There are envisioned to be 22 specific Conversomes, one for each of the 22 proteinogenic amino acids, and additional Conversome molecules for each non-proteinogenic, modified and synthetic amino acid.[000156] The Conversome molecule comprises i) a first end termed a “Decodon element” which as used herein refers to a unique, specific, single or double strand nucleic acid sequence(s); ii) a “Linker molecule” bound to the Decodon element and connecting the Decodon element and bound to iii) a “Ligamer element” at the opposite, second end which as used herein refers to a specific amino acid recognition portion of the Conversome molecule. The Ligamer element binds with a strong propensity and specificity, to its corresponding, specific, cognate amino acid which is part of the composition of a peptide,polypeptide, protein or proteome sequence(s). There can also be a “non-specific Ligamer element,” a non-specific amino acid recognition portion able to bind to any amino acid that remains open / unbound by the Ligamer element of a Conversome molecule. The Decodon strand becomes double-stranded when a first complementary strand, termed a “transDecodon strand” pairs with its complementary strand, termed “cis-Decodon strand” which is bound to the Linker element. The Decodon element can be any number of nucleic acids in length, such as at least about 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 110, 120, 130, 140, 150, 160, 170, 180, 190, 200, 210, 220, 230, 240, 250, 260, 270, 280, 290, 300, or more nucleic acids in length, at most about 300, 290, 280, 270, 260, 250, 240, 230, 220, 210, 200, 190, 180, 170, 160, 150, 140, 130, 120, 110, 100, 95, 90, 85, 80, 75, 70, 65, 60, 55, 50, 40, 35, 30, 29, 28, 27, 26, 25, 24, 23, 22, 21, 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4, 3, or 2 nucleic acids in length, ora number of nucleic acids in length that is within a range defined by any two of the preceding values. For instance, the Decodon element can be between about 2 and about 3, about 2 and about 4, about 2 and about 5, about 2 and about 6, about 2 and about 7, about 2 and about 8, about 2 and about 9, about 2 and about 10, about 2 and about 11 , about 2 and about 12, about 2 and about 13, about 2 and about 14, about 2 and about 15, about 2 and about 16, about 2 and about 17, about 2 and about 18, about 2 and about 19, about 2 and about 20, about 2 and about 21 , about 2 and about 22, about 2 and about 23, about 2 and about 24, about 2 and about 25, about 2 and about 26, about 2 and about 27, about 2 and about 28, about 2 and about 29, about 2 and about 30, about 2 and about 35, about 2 and about 40, about 25 and about 45, about 2 and about 50, about 2 and about 55, about 2 and about 60, about 2 and about 65, about 2 and about 70, about 2 and about 75, about 2 and about 80, about 2 and about 85, about 2 and about 90, about 2 and about 95, about 2 and about 100, about 2 and about 110, about 2 and about 120, about 2 and about 130, about 2 and about 140, about 2 and about 150, about 2 and about 160, about 2 and about 170, about 2 and about 180, about 2 and about 190, about 2 and about 200, about 2 and about 210, about 2 and about 220, about 2 and about 230, about 2 and about 240, about 2 and about 250, about 2 and about 260, about 2 and about 270, about 2 and about 280, about 2 and about 290, about 2 and about 300, about 3 and about 4, about 3 and about 5, about 3 and about 6, about 3 and about 7, about 3 and about 8, about 3 and about 9, about 3 and about 10, about 3 and about 11, about 3 and about 12, about 3 and about 13, about 3 and about 14, about 3 and about 15, about 3 and about 16, about 3 and about 17, about 3 and about 18, about 3 and about 19, about 3 and about 20, about 3 and about 21, about 3 and about 22, about 3 and about 23, about 3 and about 24, about 3 and about 25, about 3 and about 26, about 3 and about 27, about 3 and about 28, about 3 and about 29, about 3 and about 30,about 3 and about 35, about 3 and about 40, about 25 and about 45, about 3 and about 50, about 3 and about 55, about 3 and about 60, about 3 and about 65, about 3 and about 70, about 3 and about 75, about 3 and about 80, about 3 and about 85, about 3 and about 90, about 3 and about 95, about 3 and about 100, about 3 and about 110, about 3 and about 120, about 3 and about 130, about 3 and about 140, about 3 and about 150, about 3 and about 160, about 3 and about 170, about 3 and about 180, about 3 and about 190, about 3 and about 200, about 3 and about 210, about 3 and about 220, about 3 and about 230, about 3 and about 240, about 3 and about 250, about 3 and about 260, about 3 and about 270, about 3 and about 280, about 3 and about 290, about 3 and about 300, about 4 and about 5, about 4 and about 6, about 4 and about 7, about 4 and about 8, about 4 and about 9, about 4 and about 10, about 4 and about 11 , about 4 and about 12, about 4 and about 13, about 4 and about 14, about 4 and about 15, about 4 and about 16, about 4 and about 17, about 4 and about 18, about 4 and about 19, about 4 and about 20, about 4 and about 21 , about 4 and about 22, about 4 and about 23, about 4 and about 24, about 4 and about 25, about 4 and about 26, about 4 and about 27, about 4 and about 28, about 4 and about 29, about 4 and about 30, about 4 and about 35, about 4 and about 40, about 25 and about 45, about 4 and about 50, about 4 and about 55, about 4 and about 60, about 4 and about 65, about 4 and about 70, about 4 and about 75, about 4 and about 80, about 4 and about 85, about 4 and about 90, about 4 and about 95, about 4 and about 100, about 4 and about 110, about 4 and about 120, about 4 and about 130, about 4 and about 140, about 4 and about 150, about 4 and about 160, about 4 and about 170, about 4 and about 180, about 4 and about 190, about 4 and about 200, about 4 and about 210, about 4 and about 220, about 4 and about 230, about 4 and about 240, about 4 and about 250, about 4 and about 260, about 4 and about 270, about 4 and about 280, about 4 and about 290, about 4 and about 300, about 5 and about 6, about 5 and about 7, about 5 and about 8, about 5 and about 9, about 5 and about 10, about 5 and about 11 , about 5 and about 12, about 5 and about 13, about 5 and about 14, about 5 and about 15, about 5 and about 16, about 5 and about 17, about 5 and about 18, about 5 and about 19, about 5 and about 20, about 5 and about 21 , about 5 and about 22, about 5 and about 23, about 5 and about 24, about 5 and about 25, about 5 and about 26, about 5 and about 27, about 5 and about 28, about 5 and about 29, about 5 and about 30, about 5 and about 35, about 5 and about 40, about 25 and about 45, about 5 and about 50, about 5 and about 55, about 5 and about 60, about 5 and about 65, about 5 and about 70, about 5 and about 75, about 5 and about 80, about 5 and about 85, about 5 and about 90, about 5 and about 95, about 5 and about 100, about 5 and about 110, about 5 and about 120, about 5 and about 130, about 5 and about 140, about 5 and about 150, about 5 and about 160, about 5 and about 170, about 5 and about 180, about 5 and about 190, about 5 and about 200, about 5 and about 210, about 5 and about220, about 5 and about 230, about 5 and about 240, about 5 and about 250, about 5 and about 260, about 5 and about 270, about 5 and about 280, about 5 and about 290, about 5 and about 300, about 6 and about 7, about 6 and about 8, about 6 and about 9, about 6 and about 10, about 6 and about 11 , about 6 and about 12, about 6 and about 13, about 6 and about 14, about 6 and about 15, about 6 and about 16, about 6 and about 17, about 6 and about 18, about 6 and about 19, about 6 and about 20, about 6 and about 21, about 6 and about 22, about 6 and about 23, about 6 and about 24, about 6 and about 25, about 6 and about 26, about 6 and about 27, about 6 and about 28, about 6 and about 29, about 6 and about 30, about 6 and about 35, about 6 and about 40, about 25 and about 45, about 6 and about 50, about 6 and about 55, about 6 and about 60, about 6 and about 65, about 6 and about 70, about 6 and about 75, about 6 and about 80, about 6 and about 85, about 6 and about 90, about 6 and about 95, about 6 and about 100, about 6 and about 110, about 6 and about 120, about 6 and about 130, about 6 and about 140, about 6 and about 150, about 6 and about 160, about 6 and about 170, about 6 and about 180, about 6 and about 190, about 6 and about 200, about 6 and about 210, about 6 and about 220, about 6 and about 230, about 6 and about 240, about 6 and about 250, about 6 and about 260, about 6 and about 270, about 6 and about 280, about 6 and about 290, about 6 and about 300, about 7 and about 8, about 7 and about 9, about 7 and about 10, about 7 and about 11 , about 7 and about 12, about 7 and about 13, about 7 and about 14, about 7 and about 15, about 7 and about 16, about 7 and about 17, about 7 and about 18, about 7 and about 19, about 7 and about 20, about 7 and about 21 , about 7 and about 22, about 7 and about 23, about 7 and about 24, about 7 and about 25, about 7 and about 26, about 7 and about 27, about 7 and about 28, about 7 and about 29, about 7 and about 30, about 7 and about 35, about 7 and about 40, about 25 and about 45, about 7 and about 50, about 7 and about 55, about 7 and about 60, about 7 and about 65, about 7 and about 70, about 7 and about 75, about 7 and about 80, about 7 and about 85, about 7 and about 90, about 7 and about 95, about 7 and about 100, about 7 and about 110, about 7 and about 120, about 7 and about 130, about 7 and about 140, about 7 and about 150, about 7 and about 160, about 7 and about 170, about 7 and about 180, about 7 and about 190, about 7 and about 200, about 7 and about 210, about 7 and about 220, about 7 and about 230, about 7 and about 240, about 7 and about 250, about 7 and about 260, about 7 and about 270, about 7 and about 280, about 7 and about 290, about 7 and about 300, about 8 and about 9, about 8 and about 10, about 8 and about 11 , about 8 and about 12, about 8 and about 13, about 8 and about 14, about 8 and about 15, about 8 and about 16, about 8 and about 17, about 8 and about 18, about 8 and about 19, about 8 and about 20, about 8 and about 21 , about 8 and about 22, about 8 and about 23, about 8 and about 24, about 8 and about 25, about 8 and about 26, about 8 and about 27, about 8 and about 28, about 8 and about 29, about 8 andabout 30, about 8 and about 35, about 8 and about 40, about 25 and about 45, about 8 and about 50, about 8 and about 55, about 8 and about 60, about 8 and about 65, about 8 and about 70, about 8 and about 75, about 8 and about 80, about 8 and about 85, about 8 and about 90, about 8 and about 95, about 8 and about 100, about 8 and about 110, about 8 and about 120, about 8 and about 130, about 8 and about 140, about 8 and about 150, about 8 and about 160, about 8 and about 170, about 8 and about 180, about 8 and about 190, about 8 and about 200, about 8 and about 210, about 8 and about 220, about 8 and about 230, about 8 and about 240, about 8 and about 250, about 8 and about 260, about 8 and about 270, about 8 and about 280, about 8 and about 290, about 8 and about 300, about 9 and about 10, about 9 and about 11 , about 9 and about 12, about 9 and about 13, about 9 and about 14, about 9 and about 15, about 9 and about 16, about 9 and about 17, about 9 and about 18, about 9 and about 19, about 9 and about 20, about 9 and about 21 , about 9 and about 22, about 9 and about 23, about 9 and about 24, about 9 and about 25, about 9 and about 26, about 9 and about 27, about 9 and about 28, about 9 and about 29, about 9 and about 30, about 9 and about 35, about 9 and about 40, about 25 and about 45, about 9 and about 50, about 9 and about 55, about 9 and about 60, about 9 and about 65, about 9 and about 70, about 9 and about 75, about 9 and about 80, about 9 and about 85, about 9 and about 90, about 9 and about 95, about 9 and about 100, about 9 and about 110, about 9 and about 120, about 9 and about 130, about 9 and about 140, about 9 and about 150, about 9 and about 160, about 9 and about 170, about 9 and about 180, about 9 and about 190, about 9 and about 200, about 9 and about 210, about 9 and about 220, about 9 and about 230, about 9 and about 240, about 9 and about 250, about 9 and about 260, about 9 and about 270, about 9 and about 280, about 9 and about 290, about 9 and about 300, about 10 and about 11 , about 10 and about 12, about 10 and about 13, about 10 and about 14, about 10 and about 15, about 10 and about 16, about 10 and about 17, about 10 and about 18, about 10 and about 19, about 10 and about 20, about 10 and about 21, about 10 and about 22, about 10 and about 23, about 10 and about 24, about 10 and about 25, about 10 and about 26, about 10 and about 27, about 10 and about 28, about 10 and about 29, about 10 and about 30, about 10 and about 35, about 10 and about 40, about 25 and about 45, about 10 and about 50, about 10 and about 55, about 10 and about 60, about 10 and about 65, about 10 and about 70, about 10 and about 75, about 10 and about 80, about 10 and about 85, about 10 and about 90, about 10 and about 95, about 10 and about 100, about 10 and about 110, about 10 and about 120, about 10 and about 130, about 10 and about 140, about 10 and about 150, about 10 and about 160, about 10 and about 170, about 10 and about 180, about 10 and about 190, about 10 and about 200, about 10 and about 210, about 10 and about 220, about 10 and about 230, about 10 and about 240, about 10 and about 250, about 10 and about 260, about 10 and about 270,about 10 and about 280, about 10 and about 290, about 10 and about 300, about 11 and about 12, about 11 and about 13, about 11 and about 14, about 11 and about 15, about 11 and about 16, about 11 and about 17, about 11 and about 18, about 11 and about 19, about 11 and about 20, about 11 and about 21 , about 11 and about 22, about 11 and about 23, about 11 and about 24, about 11 and about 25, about 11 and about 26, about 11 and about 27, about 11 and about 28, about 11 and about 29, about 11 and about 30, about 11 and about 35, about 11 and about 40, about 25 and about 45, about 11 and about 50, about 11 and about 55, about 11 and about 60, about 11 and about 65, about 11 and about 70, about 11 and about 75, about 11 and about 80, about 11 and about 85, about 11 and about 90, about 11 and about 95, about 11 and about 100, about 11 and about 110, about 11 and about 120, about 11 and about 130, about 11 and about 140, about 11 and about 150, about 11 and about 160, about 11 and about 170, about 11 and about 180, about 11 and about 190, about 11 and about 200, about 11 and about 210, about 11 and about 220, about 11 and about 230, about 11 and about 240, about 11 and about 250, about 11 and about 260, about 11 and about 270, about 11 and about 280, about 11 and about 290, about 11 and about 300, about 12 and about 13, about 12 and about 14, about 12 and about 15, about 12 and about 16, about 12 and about 17, about 12 and about 18, about 12 and about 19, about 12 and about 20, about 12 and about 21, about 12 and about 22, about 12 and about 23, about 12 and about 24, about 12 and about 25, about 12 and about 26, about 12 and about 27, about 12 and about 28, about 12 and about 29, about 12 and about 30, about 12 and about 35, about 12 and about 40, about 25 and about 45, about 12 and about 50, about 12 and about 55, about 12 and about 60, about 12 and about 65, about 12 and about 70, about 12 and about 75, about 12 and about 80, about 12 and about 85, about 12 and about 90, about 12 and about 95, about 12 and about 100, about 12 and about 110, about 12 and about 120, about 12 and about 130, about 12 and about 140, about 12 and about 150, about 12 and about 160, about 12 and about 170, about 12 and about 180, about 12 and about 190, about 12 and about 200, about 12 and about 210, about 12 and about 220, about 12 and about 230, about 12 and about 240, about 12 and about 250, about 12 and about 260, about 12 and about 270, about 12 and about 280, about 12 and about 290, about 12 and about 300, about 13 and about 14, about 13 and about 15, about 13 and about 16, about 13 and about 17, about 13 and about 18, about 13 and about 19, about 13 and about 20, about 13 and about 21 , about 13 and about 22, about 13 and about 23, about 13 and about 24, about 13 and about 25, about 13 and about 26, about 13 and about 27, about 13 and about 28, about 13 and about 29, about 13 and about 30, about 13 and about 35, about 13 and about 40, about 25 and about 45, about 13 and about 50, about 13 and about 55, about 13 and about 60, about 13 and about 65, about 13 and about 70, about 13 and about 75, about 13 and about 80, about 13 and about85, about 13 and about 90, about 13 and about 95, about 13 and about 100, about 13 and about 110, about 13 and about 120, about 13 and about 130, about 13 and about 140, about 13 and about 150, about 13 and about 160, about 13 and about 170, about 13 and about 180, about 13 and about 190, about 13 and about 200, about 13 and about 210, about 13 and about 220, about 13 and about 230, about 13 and about 240, about 13 and about 250, about 13 and about 260, about 13 and about 270, about 13 and about 280, about 13 and about 290, about 13 and about 300, about 14 and about 15, about 14 and about 16, about 14 and about 17, about 14 and about 18, about 14 and about 19, about 14 and about 20, about 14 and about 21 , about 14 and about 22, about 14 and about 23, about 14 and about 24, about 14 and about 25, about 14 and about 26, about 14 and about 27, about 14 and about 28, about 14 and about 29, about 14 and about 30, about 14 and about 35, about 14 and about 40, about 25 and about 45, about 14 and about 50, about 14 and about 55, about 14 and about 60, about 14 and about 65, about 14 and about 70, about 14 and about 75, about 14 and about 80, about 14 and about 85, about 14 and about 90, about 14 and about 95, about 14 and about 100, about 14 and about 110, about 14 and about 120, about 14 and about 130, about 14 and about 140, about 14 and about 150, about 14 and about 160, about 14 and about 170, about 14 and about 180, about 14 and about 190, about 14 and about 200, about 14 and about 210, about 14 and about 220, about 14 and about 230, about 14 and about 240, about 14 and about 250, about 14 and about 260, about 14 and about 270, about 14 and about 280, about 14 and about 290, about 14 and about 300, about 15 and about 16, about 15 and about 17, about 15 and about 18, about 15 and about 19, about 15 and about 20, about 15 and about 21, about 15 and about 22, about 15 and about 23, about 15 and about 24, about 15 and about 25, about 15 and about 26, about 15 and about 27, about 15 and about 28, about 15 and about 29, about 15 and about 30, about 15 and about 35, about 15 and about 40, about 25 and about 45, about 15 and about 50, about 15 and about 55, about 15 and about 60, about 15 and about 65, about 15 and about 70, about 15 and about 75, about 15 and about 80, about 15 and about 85, about 15 and about 90, about 15 and about 95, about 15 and about 100, about 15 and about 110, about 15 and about 120, about 15 and about 130, about 15 and about 140, about 15 and about 150, about 15 and about 160, about 15 and about 170, about 15 and about 180, about 15 and about 190, about 15 and about 200, about 15 and about 210, about 15 and about 220, about 15 and about 230, about 15 and about 240, about 15 and about 250, about 15 and about 260, about 15 and about 270, about 15 and about 280, about 15 and about 290, about 15 and about 300, about 16 and about 17, about 16 and about 18, about 16 and about 19, about 16 and about 20, about 16 and about 21, about 16 and about 22, about 16 and about 23, about 16 and about 24, about 16 and about 25, about 16 and about 26, about 16 and about 27, about 16 and about 28, about 16 andabout 29, about 16 and about 30, about 16 and about 35, about 16 and about 40, about 25 and about 45, about 16 and about 50, about 16 and about 55, about 16 and about 60, about 16 and about 65, about 16 and about 70, about 16 and about 75, about 16 and about 80, about 16 and about 85, about 16 and about 90, about 16 and about 95, about 16 and about 100, about 16 and about 110, about 16 and about 120, about 16 and about 130, about 16 and about 140, about 16 and about 150, about 16 and about 160, about 16 and about 170, about 16 and about 180, about 16 and about 190, about 16 and about 200, about 16 and about 210, about 16 and about 220, about 16 and about 230, about 16 and about 240, about 16 and about 250, about 16 and about 260, about 16 and about 270, about 16 and about 280, about 16 and about 290, about 16 and about 300, about 17 and about 18, about 17 and about 19, about 17 and about 20, about 17 and about 21, about 17 and about 22, about 17 and about 23, about 17 and about 24, about 17 and about 25, about 17 and about 26, about 17 and about 27, about 17 and about 28, about 17 and about 29, about 17 and about 30, about 17 and about 35, about 17 and about 40, about 25 and about 45, about 17 and about 50, about 17 and about 55, about 17 and about 60, about 17 and about 65, about 17 and about 70, about 17 and about 75, about 17 and about 80, about 17 and about 85, about 17 and about 90, about 17 and about 95, about 17 and about 100, about 17 and about 110, about 17 and about 120, about 17 and about 130, about 17 and about 140, about 17 and about 150, about 17 and about 160, about 17 and about 170, about 17 and about 180, about 17 and about 190, about 17 and about 200, about 17 and about 210, about 17 and about 220, about 17 and about 230, about 17 and about 240, about 17 and about 250, about 17 and about 260, about 17 and about 270, about 17 and about 280, about 17 and about 290, about 17 and about 300, about 18 and about 19, about 18 and about 20, about 18 and about 21, about 18 and about 22, about 18 and about 23, about 18 and about 24, about 18 and about 25, about 18 and about 26, about 18 and about 27, about 18 and about 28, about 18 and about 29, about 18 and about 30, about 18 and about 35, about 18 and about 40, about 25 and about 45, about 18 and about 50, about 18 and about 55, about 18 and about 60, about 18 and about 65, about 18 and about 70, about 18 and about 75, about 18 and about 80, about 18 and about 85, about 18 and about 90, about 18 and about 95, about 18 and about 100, about 18 and about 110, about 18 and about 120, about 18 and about 130, about 18 and about 140, about 18 and about 150, about 18 and about 160, about 18 and about 170, about 18 and about 180, about 18 and about 190, about 18 and about 200, about 18 and about 210, about 18 and about 220, about 18 and about 230, about 18 and about 240, about 18 and about 250, about 18 and about 260, about 18 and about 270, about 18 and about 280, about 18 and about 290, about 18 and about 300, about 19 and about 20, about 19 and about 21 , about 19 and about 22, about 19 and about 23, about 19 and about 24, about 19 and about 25, about 19and about 26, about 19 and about 27, about 19 and about 28, about 19 and about 29, about 19 and about 30, about 19 and about 35, about 19 and about 40, about 25 and about 45, about 19 and about 50, about 19 and about 55, about 19 and about 60, about 19 and about 65, about 19 and about 70, about 19 and about 75, about 19 and about 80, about 19 and about 85, about 19 and about 90, about 19 and about 95, about 19 and about 100, about 19 and about 110, about 19 and about 120, about 19 and about 130, about 19 and about 140, about 19 and about 150, about 19 and about 160, about 19 and about 170, about 19 and about 180, about 19 and about 190, about 19 and about 200, about 19 and about 210, about 19 and about 220, about 19 and about 230, about 19 and about 240, about 19 and about 250, about 19 and about 260, about 19 and about 270, about 19 and about 280, about 19 and about 290, about 19 and about 300, about 20 and about 21 , about 20 and about 22, about 20 and about 23, about 20 and about 24, about 20 and about 25, about 20 and about 26, about 20 and about 27, about 20 and about 28, about 20 and about 29, about 20 and about 30, about 20 and about 35, about 20 and about 40, about 25 and about 45, about 20 and about 50, about 20 and about 55, about 20 and about 60, about 20 and about 65, about 20 and about 70, about 20 and about 75, about 20 and about 80, about 20 and about 85, about 20 and about 90, about 20 and about 95, about 20 and about 100, about 20 and about 110, about 20 and about 120, about 20 and about 130, about 20 and about 140, about 20 and about 150, about 20 and about 160, about 20 and about 170, about 20 and about 180, about 20 and about 190, about 20 and about 200, about 20 and about 210, about 20 and about 220, about 20 and about 230, about 20 and about 240, about 20 and about 250, about 20 and about 260, about 20 and about 270, about 20 and about 280, about 20 and about 290, about 20 and about 300, about 21 and about 22, about 21 and about 23, about 21 and about 24, about 21 and about 25, about 21 and about 26, about 21 and about 27, about 21 and about 28, about 21 and about 29, about 21 and about 30, about 21 and about 35, about 21 and about 40, about 25 and about 45, about 21 and about 50, about 21 and about 55, about 21 and about 60, about 21 and about 65, about 21 and about 70, about 21 and about 75, about 21 and about 80, about 21 and about 85, about 21 and about 90, about 21 and about 95, about 21 and about 100, about 21 and about 110, about 21 and about 120, about 21 and about 130, about 21 and about 140, about 21 and about 150, about 21 and about 160, about 21 and about 170, about 21 and about 180, about 21 and about 190, about 21 and about 200, about 21 and about 210, about 21 and about 220, about 21 and about 230, about 21 and about 240, about 21 and about 250, about 21 and about 260, about 21 and about 270, about 21 and about 280, about 21 and about 290, about 21 and about 300, about 22 and about 23, about 22 and about 24, about 22 and about 25, about 22 and about 26, about 22 and about 27, about 22 and about 28, about 22 and about 29, about 22 and about 30, about 22 and about 35,about 22 and about 40, about 25 and about 45, about 22 and about 50, about 22 and about 55, about 22 and about 60, about 22 and about 65, about 22 and about 70, about 22 and about 75, about 22 and about 80, about 22 and about 85, about 22 and about 90, about 22 and about 95, about 22 and about 100, about 22 and about 110, about 22 and about 120, about 22 and about 130, about 22 and about 140, about 22 and about 150, about 22 and about 160, about 22 and about 170, about 22 and about 180, about 22 and about 190, about 22 and about 200, about 22 and about 210, about 22 and about 220, about 22 and about 230, about 22 and about 240, about 22 and about 250, about 22 and about 260, about 22 and about 270, about 22 and about 280, about 22 and about 290, about 22 and about 300, about 23 and about 24, about 23 and about 25, about 23 and about 26, about 23 and about 27, about 23 and about 28, about 23 and about 29, about 23 and about 30, about 23 and about 35, about 23 and about 40, about 25 and about 45, about 23 and about 50, about 23 and about 55, about 23 and about 60, about 23 and about 65, about 23 and about 70, about 23 and about 75, about 23 and about 80, about 23 and about 85, about 23 and about 90, about 23 and about 95, about 23 and about 100, about 23 and about 110, about 23 and about 120, about 23 and about 130, about 23 and about 140, about 23 and about 150, about 23 and about 160, about 23 and about 170, about 23 and about 180, about 23 and about 190, about 23 and about 200, about 23 and about 210, about 23 and about 220, about 23 and about 230, about 23 and about 240, about 23 and about 250, about 23 and about 260, about 23 and about 270, about 23 and about 280, about 23 and about 290, about 23 and about 300, about 24 and about 25, about 24 and about 26, about 24 and about 27, about 24 and about 28, about 24 and about 29, about 24 and about 30, about 24 and about 35, about 24 and about 40, about 25 and about 45, about 24 and about 50, about 24 and about 55, about 24 and about 60, about 24 and about 65, about 24 and about 70, about 24 and about 75, about 24 and about 80, about 24 and about 85, about 24 and about 90, about 24 and about 95, about 24 and about 100, about 24 and about 110, about 24 and about 120, about 24 and about 130, about 24 and about 140, about 24 and about 150, about 24 and about 160, about 24 and about 170, about 24 and about 180, about 24 and about 190, about 24 and about 200, about 24 and about 210, about 24 and about 220, about 24 and about 230, about 24 and about 240, about 24 and about 250, about 24 and about 260, about 24 and about 270, about 24 and about 280, about 24 and about 290, about 24 and about 300, about 25 and about 26, about 25 and about 27, about 25 and about 28, about 25 and about 29, about 25 and about 30, about 25 and about 35, about 25 and about 40, about 25 and about 45, about 25 and about 50, about 25 and about 55, about 25 and about 60, about 25 and about 65, about 25 and about 70, about 25 and about 75, about 25 and about 80, about 25 and about 85, about 25 and about 90, about 25 and about 95, about 25 and about 100, about25 and about 110, about 25 and about 120,about 25 and about 130, about 25 and about 140, about 25 and about 150, about 25 and about 160, about 25 and about 170, about 25 and about 180, about 25 and about 190, about 25 and about 200, about 25 and about 210, about 25 and about 220, about 25 and about 230, about 25 and about 240, about 25 and about 250, about 25 and about 260, about 25 and about 270, about 25 and about 280, about 25 and about 290, about 25 and about 300, about 26 and about 27, about 26 and about 28, about 26 and about 29, about 26 and about 30, about 26 and about 35, about 26 and about 40, about 26 and about 45, about 26 and about 50, about 26 and about 55, about 26 and about 60, about 26 and about 65, about 26 and about 70, about 26 and about 75, about 26 and about 80, about 26 and about 85, about 26 and about 90, about 26 and about 95, about 26 and about 100, about 26 and about 110, about 26 and about 120, about 26 and about 130, about 26 and about 140, about 26 and about 150, about 26 and about 160, about 26 and about 170, about 26 and about 180, about 26 and about 190, about 26 and about 200, about 26 and about 210, about 26 and about 220, about 26 and about 230, about 26 and about 240, about 26 and about 250, about 26 and about 260, about 26 and about 270, about 26 and about 280, about 26 and about 290, about 26 and about 300, about 27 and about 28, about 27 and about 29, about 27 and about 30, about 27 and about 35, about 27 and about 40, about 27 and about 45, about 27 and about 5, about 27 and about 55, about 27 and about 60, about 27 and about 65, about 27 and about 70, about 27 and about 75, about 27 and about 80, about 27 and about 85, about 27 and about 90, about 27 and about 95, about 27 and about 100, about 27 and about 110, about 27 and about 120, about 27 and about 130, about 27 and about 140, about 27 and about 150, about 27 and about 160, about 27 and about 170, about 27 and about 180, about 27 and about 190, about 27 and about 200, about 27 and about 210, about 27 and about 220, about 27 and about 230, about 27 and about 240, about 27 and about 250, about 27 and about 260, about 27 and about 270, about 27 and about 280, about 27 and about 290, about 27 and about 300, about 28 and about 29, about 28 and about 30, about 28 and about 35, about 28 and about 40, about 28 and about 45, about 28 and about 50, about 28 and about 55, about 28 and about 60, about 28 and about 65, about 28 and about 70, about 28 and about 75, about 28 and about 80, about 28 and about 85, about 28 and about 90, about 28 and about 95, about 28 and about 100, about 28 and about 110, about 28 and about 120, about 28 and about 130, about 28 and about 140, about 28 and about 150, about 28 and about 160, about 28 and about 170, about 28 and about 180, about 28 and about 190, about 28 and about 200, about 28 and about 210, about 28 and about 220, about 28 and about 230, about 28 and about 240, about 28 and about 250, about 28 and about 260, about 28 and about 270, about 28 and about 280, about 28 and about 290, about 28 and about 300, about 29 and about 30, about 29 and about 35, about 29 and about 40, about 29 and about 45, about 29 and about 50, about 29and about 55, about 29 and about 60, about 29 and about 65, about 29 and about 70, about 29 and about 75, about 29 and about 80, about 29 and about 85, about 29 and about 90, about 29 and about 95, about 29 and about 100, about 29 and about 110, about 29 and about 120, about 29 and about 130, about 29 and about 140, about 29 and about 150, about 29 and about 160, about 29 and about 170, about 29 and about 180, about 29 and about 190, about 29 and about 200, about 29 and about 210, about 29 and about 220, about 29 and about 230, about 29 and about 240, about 29 and about 250, about 29 and about 260, about 29 and about 270, about 29 and about 280, about 29 and about 290, about 29 and about 300, about 30 and about 35, about 30 and about 40, about 30 and about 45, about 30 and about 50, about 30 and about 55, about 30 and about 60, about 30 and about 65, about 30 and about 70, about 30 and about 75, about 30 and about 80, about 30 and about 85, about 30 and about 90, about 30 and about 95, about 30 and about 100, about 30 and about 110, about 30 and about 120, about 30 and about 130, about 30 and about 140, about 30 and about 150, about 30 and about 160, about 30 and about 170, about 30 and about 180, about 30 and about 190, about 30 and about 200, about 30 and about 210, about 30 and about 220, about 30 and about 230, about 30 and about 240, about 30 and about 250, about 30 and about 260, about 30 and about 270, about 30 and about 280, about 30 and about 290, about 30 and about 300, about 35 and about 40, about 35 and about 45, about 35 and about 50, about 35 and about 55, about 35 and about 60, about 35 and about 65, about 35 and about 70, about 35 and about 75, about 35 and about 80, about 35 and about 85, about 35 and about 90, about 35 and about 95, about 35 and about 100, about 35 and about 110, about 35 and about 120, about 35 and about 130, about 35 and about 140, about 35 and about 150, about 35 and about 160, about 35 and about 170, about 35 and about 180, about 35 and about 190, about 35 and about 200, about 35 and about 210, about 35 and about 220, about 35 and about 230, about 35 and about 240, about 35 and about 250, about 35 and about 260, about 35 and about 270, about 35 and about 280, about 35 and about 290, about 35 and about 300, about 40 and about 45, about 40 and about 45, about 40 and about 55, about 40 and about 60, about 40 and about 65, about 40 and about 70, about 40 and about 75, about 40 and about 80, about 40 and about 85, about 40 and about 90, about 40 and about 95, about 40 and about 100, about 40 and about 110, about 40 and about 120, about 40 and about 130, about 40 and about 140, about 40 and about 150, about 40 and about 160, about 40 and about 170, about 40 and about 180, about 40 and about 190, about 40 and about 200, about 40 and about 210, about 40 and about 220, about 40 and about 230, about 40 and about 240, about 40 and about 250, about 40 and about 260, about 40 and about 270, about 40 and about 280, about 40 and about 290, about 40 and about 300, about 45 and about 50, about 45 and about 55, about 45 and about 60, about 45 and about 65, about 45 and about 70,about 45 and about 75, about 45 and about 80, about 45 and about 85, about 45 and about 90, about 45 and about 95, about 45 and about 100, about 45 and about 110, about 45 and about 120, about 45 and about 130, about 45 and about 140, about 45 and about 150, about 45 and about 160, about 45 and about 170, about 45 and about 180, about 45 and about 190, about 45 and about 200, about 45 and about 210, about 45 and about 220, about 45 and about 230, about 45 and about 240, about 45 and about 250, about 45 and about 260, about 45 and about 270, about 45 and about 280, about 45 and about 290, about 45 and about 300, about 50 and about 55, about 50 and about 60, about 50 and about 65, about 50 and about 70, about 50 and about 75, about 50 and about 80, about 50 and about 85, about 50 and about 90, about 50 and about 95, about 50 and about 100, about 50 and about 110, about 50 and about 120, about 50 and about 130, about 50 and about 140, about 50 and about 150, about 50 and about 160, about 50 and about 170, about 50 and about 180, about 50 and about 190, about 50 and about 200, about 50 and about 210, about 50 and about 220, about 50 and about 230, about 50 and about 240, about 50 and about 250, about 50 and about 260, about 50 and about 270, about 50 and about 280, about 50 and about 290, about 50 and about 300, about 55 and about 60, about 55 and about 65, about 55 and about 70, about 55 and about 75, about 55 and about 80, about 55 and about 85, about 55 and about 90, about 55 and about 95, about 55 and about 100, about 55 and about 110, about 55 and about 120, about 55 and about 130, about 55 and about 140, about 55 and about 150, about 55 and about 160, about 55 and about 170, about 55 and about 180, about 55 and about 190, about 55 and about 200, about 55 and about 210, about 55 and about 220, about 55 and about 230, about 55 and about 240, about 55 and about 250, about 55 and about 260, about 55 and about 270, about 55 and about 280, about 55 and about 290, about 55 and about 300, about 60 and about 65, about 60 and about 70, about 60 and about 75, about 60 and about 80, about 60 and about 85, about 60 and about 90, about 60 and about 95, about 60 and about 100, about 60 and about 110, about 60 and about 120, about 60 and about 130, about 60 and about 140, about 60 and about 150, about 60 and about 160, about 60 and about 170, about 60 and about 180, about 60 and about 190, about 60 and about 200, about 60 and about 210, about 60 and about 220, about 60 and about 230, about 60 and about 240, about 60 and about 250, about 60 and about 260, about 60 and about 270, about 60 and about 280, about 60 and about 290, about 60 and about 300, about 65 and about 70, about 65 and about 75, about 65 and about 80, about 65 and about 85, about 65 and about 90, about 65 and about 95, about 65 and about 100, about 65 and about 110, about 65 and about 120, about 65 and about 130, about 65 and about 140, about 65 and about 150, about 65 and about 160, about 65 and about 170, about 65 and about 180, about 65 and about 190, about 65 and about 200, about 65 and about 210, about 65 and about 220, about 65 andabout 230, about 65 and about 240, about 65 and about 250, about 65 and about 260, about 65 and about 270, about 65 and about 280, about 65 and about 290, about 65 and about 300, about 70 and about 75, about 70 and about 80, about 70 and about 85, about 70 and about 90, about 70 and about 95, about 70 and about 100, about 70 and about 110, about 70 and about 120, about 70 and about 130, about 70 and about 140, about 70 and about 150, about 70 and about 160, about 70 and about 170, about 70 and about 180, about 70 and about 190, about 70 and about 200, about 70 and about 210, about 70 and about 220, about 70 and about 230, about 70 and about 240, about 70 and about 250, about 70 and about 260, about 70 and about 270, about 70 and about 280, about 70 and about 290, about 70 and about 300, about 75 and about 80, about 75 and about 85, about 75 and about 90, about 75 and about 95, about 75 and about 100, about 75 and about 110, about 75 and about 120, about 75 and about 130, about 75 and about 140, about 75 and about 150, about 75 and about 160, about 75 and about 170, about 75 and about 180, about 75 and about 190, about 75 and about 200, about 75 and about 210, about 75 and about 220, about 75 and about 230, about 75 and about 240, about 75 and about 250, about 75 and about 260, about 75 and about 270, about 75 and about 280, about 75 and about 290, about 75 and about 300, about 80 and about 85, about 80 and about 90, about 80 and about 95, about 80 and about 100, about 80 and about 110, about 80 and about 120, about 80 and about 130, about 80 and about 140, about 80 and about 150, about 80 and about 160, about 80 and about 170, about 80 and about 180, about 80 and about 190, about 80 and about 200, about 80 and about 210, about 80 and about 220, about 80 and about 230, about 80 and about 240, about 80 and about 250, about 80 and about 260, about 80 and about 270, about 80 and about 280, about 80 and about 290, about 80 and about 300, about 85 and about 90, about 85 and about 95, about 85 and about 100, about 85 and about 110, about 85 and about 120, about 85 and about 130, about 85 and about 140, about 85 and about 150, about 85 and about 160, about 85 and about 170, about 85 and about 180, about 85 and about 190, about 85 and about 200, about 85 and about 210, about 85 and about 220, about 85 and about 230, about 85 and about 240, about 85 and about 250, about 85 and about 260, about 85 and about 270, about 85 and about 280, about 85 and about 290, about 85 and about 300, about 90 and about 95, about 90 and about 100, about 90 and about 110, about 90 and about 120, about 90 and about 130, about 90 and about 140, about 90 and about 150, about 90 and about 160, about 90 and about 170, about 90 and about 180, about 90 and about 190, about 90 and about 200, about 90 and about 210, about 90 and about 220, about 90 and about 230, about 90 and about 240, about 90 and about 250, about 90 and about 260, about 90 and about 270, about 90 and about 280, about 90 and about 290, about 90 and about 300, about 95 and about 100, about 95 and about 110, about 95 and about 120, about 95 and about 130,about 95 and about 140, about 95 and about 150, about 95 and about 160, about 95 and about 170, about 95 and about 180, about 95 and about 190, about 95 and about 200, about 95 and about 210, about 95 and about 220, about 95 and about 230, about 95 and about 240, about 95 and about 250, about 95 and about 260, about 95 and about 270, about 95 and about 280, about 95 and about 290, about 95 and about 300, about 100 and about 110, about 100 and about 120, about 100 and about 130, about 100 and about 140, about 100 and about 150, about 100 and about 160, about 100 and about 170, about 100 and about 180, about 100 and about 190, about 100 and about 200, about 100 and about 210, about 100 and about 220, about 100 and about 230, about 100 and about 240, about 100 and about 250, about 100 and about 260, about 100 and about 270, about 100 and about 280, about 100 and about 290, about 100 and about 300, about 110 and about 120, about 110 and about 130, about 110 and about 140, about 110 and about 150, about 110 and about 160, about 110 and about 170, about 110 and about 180, about 110 and about 190, about 110 and about 200, about 110 and about 210, about 110 and about 220, about 110 and about 230, about 110 and about 240, about 110 and about 250, about 110 and about 260, about 110 and about 270, about 110 and about 280, about 110 and about 290, about 110 and about 300, about 120 and about 130, about 120 and about 140, about 120 and about 150, about 120 and about 160, about 120 and about 170, about 120 and about 180, about 120 and about 190, about 120 and about 200, about 120 and about 210, about 120 and about 220, about 120 and about 230, about 120 and about 240, about 120 and about 250, about 120 and about 260, about 120 and about 270, about 120 and about 280, about 120 and about 290, about 120 and about 300, about 130 and about 140, about 130 and about 150, about 130 and about 160, about 130 and about 170, about 130 and about 180, about 130 and about 190, about 130 and about 200, about 130 and about 210, about 130 and about 220, about 130 and about 230, about 130 and about 240, about 130 and about 250, about 130 and about 260, about 130 and about 270, about 130 and about 280, about 130 and about 290, about 130 and about 300, about 140 and about 150, about 140 and about 160, about 140 and about 170, about 140 and about 180, about 140 and about 190, about 140 and about 200, about 140 and about 210, about 140 and about 220, about 140 and about 230, about 140 and about 240, about 140 and about 250, about 140 and about 260, about 140 and about 270, about 140 and about 280, about 140 and about 290, about 140 and about 300, about 150 and about 160, about 150 and about 170, about 150 and about 180, about 150 and about 190, about 150 and about 200, about 150 and about 210, about 150 and about 220, about 150 and about 230, about 150 and about240, about 150 and about 250, about 150 and about 260, about 150 and about 270, about 150 and about 280, about 150 and about 290, about 150 and about 300, about 160 and about 170, about 160 and about 180, about 160 and about 190, about 160 and about 200, about 160and about 210, about 160 and about 220, about 160 and about 230, about 160 and about 240, about 160 and about 250, about 160 and about 260, about 160 and about 270, about 160 and about 280, about 160 and about 290, about 160 and about 300, about 170 and about 180, about 170 and about 190, about 170 and about 200, about 170 and about 210, about 170 and about 220, about 170 and about 230, about 170 and about 240, about 170 and about 250, about 170 and about 260, about 170 and about 270, about 170 and about 280, about 170 and about 290, about 170 and about 300, about 180 and about 190, about 180 and about 200, about 180 and about 210, about 180 and about 220, about 180 and about 230, about 180 and about 240, about 180 and about 250, about 180 and about 260, about 180 and about 270, about 180 and about 280, about 180 and about 290, about 180 and about 300, about 190 and about 200, about 190 and about 210, about 190 and about 220, about 190 and about 230, about 190 and about 240, about 190 and about 250, about 190 and about 260, about 190 and about 270, about 190 and about 280, about 190 and about 290, about 190 and about 300, about 200 and about 210, about 200 and about 220, about 200 and about 230, about 200 and about 240, about 200 and about 250, about 200 and about 260, about 200 and about 270, about 200 and about 280, about 200 and about 290, about 200 and about 300, about 210 and about 220, about 210 and about 230, about 210 and about 240, about 210 and about 250, about 210 and about 260, about 210 and about 270, about 210 and about 280, about 210 and about 290, about 210 and about 300, about 220 and about 230, about 220 and about 240, about 220 and about 250, about 220 and about 260, about 220 and about 270, about 220 and about 280, about 220 and about 290, about 220 and about 300, about 230 and about 240, about 230 and about 250, about 230 and about 260, about 230 and about 270, about 230 and about 280, about 230 and about 290, about 230 and about 300, about 240 and about 250, about 240 and about 260, about 240 and about 270, about 240 and about 280, about 240 and about 290, about 240 and about 300, about 250 and about 260, about 250 and about 270, about 250 and about 280, about 250 and about 290, about 250 and about 300, about 260 and about 270, about 260 and about 280, about 260 and about 290, about 260 and about 300, about 270 and about 280, about 270 and about 290, about 270 and about 300, about 280 and about 290, about 280 and about 300, or about 290 and about 300 nucleic acids in length.[000157] Binding of the Ligamer to its specific amino acid can be facilitated by chemical or physical means coming from denaturing and / or fragmentation of the polypeptide, protein or proteome into an unfolded polypeptide, protein, proteome an / or peptide sequence(s). The unfolding or fragmentation can render each Ligamer’s target amino acid more accessible for binding by its specific Ligamer amino acid recognition portion.[000158] Use of a mixture of a plurality of Conversome molecules facilitates reverse translation of polypeptide(s)’, protein(s)’, proteome(s)’, and peptide(s)’ amino acid sequence(s) into corresponding encoding DNA oligonucleotide nucleic acid sequence(s), termed pDNA(s), in a single reaction vessel simultaneously. This involves each Conversome molecule to both bind its Ligamer’s amino acid recognition portion to the Ligamer’s cognate amino acid(s) and the concatenation by either a ligation enzyme or a chemical means each of the Decodon strand’(s),’ in a spatial alignment that permits interlocking and concatenation to one another, together via ligating either i) a single-strand cis-Decodon; ii) a single strand trans- Decodon; or both iii) a cis-Decodon bound to its complementary trans-Decodon to each other bound Conversomes’ i) single-strand cis-Decodon; ii) single strand trans-Decodon; or both iii) a cis-Decodon bound to its complementary trans-Decodon sequence(s) to form a “pDNA” sequence(s).[000159] “pDNA” stands for protein-derived DNA nucleic acid sequence(s). The resulting pDNA nucleic acid sequence(s) can be used in methods of protein detection, quantitation, identification, protein discovery, discovering new protein modification positions, and quantitating the amount and type of protein modifications via qPCR, Next Generation Sequencing (NGS), digital PGR, Sanger Sequencing and other methods for protein analyses as is known to the skilled artisan.[000160] “pRNA” stands for protein-derived RNA nucleic acid sequence(s). The resulting pRNA nucleic acid sequence(s) can be used in methods of protein: detection, quantitation, identification, protein discovery, discovering new protein modification positions, and quantitating the amount and type of protein modifications via qPCR, Next Generation Sequencing (NGS), digital PGR, Sanger Sequencing and other methods for protein analyses as is known to the skilled artisan.[000161] Furthermore, the Conversome molecules can also replace affinity reagents in some applications, including, but not limited to, ELISA, Western blots, Proximity Ligation Assay (PLA), Proximity Extension Assay (PEA), Protein arrays, and Gels as would be known to the skilled artisan.[000162] “Conversome molecules” can also assist in assessing protein:protein interactions and structural arrangements. As is illustrated in Figs. 13A-13F proteins, in their natural state, are actively interacting with one another and are folded into regions where each protein’s amino acids’ would be accessible for binding by Conversome molecules’ Ligamers. The concatenation of Decodons which are in an interlocking spatial arrangement that permits interlocking and concatenation to each other can be used to establish a “pattern” based on the Conversomes that are close to each other (Fig. 13E) which form the pDNA sequence strand when their Decodon strands concatenate. Monitoring the proteins’structures and interactions can result in changes in the “pattern” as changes in structure will change which Conversomes can concatenate to one another, which is seen as a change in the “pattern” versus the pattern from earlier proteins’ interactions.[000163] As illustrated in Figures 12F and 13F the denaturation of the pDNA sequence strand (1210) (concatenated trans-Decodon from the cis-Decodon DNA (1200) and detection of the concatenated nucleic acid by NGS, qPCR or using a fluor or enzyme, or enriched via immunoprecipitation, or captured if a magnetic bead (or other affinity reagent) is attached to the pDNA can elucidate protein interactions as well as structural confirmation changes in the one, two or more proteins which are interacting in their native environment or with one another.[000164] The phrases “cis-Decodon strand” and “cis-Decodon” are used interchangeably herein and refer to at least one of: i) the single-stranded nucleic acid sequence strand within the Decodon element at the first end of a Conversome molecule and / or the “cis-Decodon strand” connecting the Decodon element to the Linker and / or the double-stranded nucleic acid sequence strand within the Decodon element binding to the complementary “trans-Decodon strand”. The cis-Decodon strand comprises any number of nucleic acids in length described herein with respect to Decodon elements and can be a unique, specific, single or double strand nucleic acid sequence(s)selected from at least one nucleic acid type or a mixture of nucleic acids including, but not limited to, Deoxyribonucleic Acid (DNA), Ribonucleic Acid (RNA), Locked Nucleic Acid (LNA) Peptide Nucleic Acid (PNA), Threose Nucleic Acid (TNA), Glycol Nucleic Acid (GNA), 1,5-Anhydrohexitol nucleic acid (HNA), Cyclohexene nucleic acid (CeNA), and Fluoroarabino nucleic acid (FANA) base(s) and / or sequences. The cis-Decodon when paired with the Ligamer element, at the opposite second end of the Conversome molecule, provides the unique, identifying nucleic acid sequence for each of the cognate specific amino acids bound specifically by the Ligamer element’s specific amino acid recognition portion.[000165] The phrases “trans-Decodon strand” and “trans-Decodon” are used interchangeably herein and refer to the single-stranded nucleic acid sequence strand within the Decodon element at the first end of a Conversome molecule and / or the doublestranded nucleic acid sequence strand within the Decodon element binding to the complementary “cis-Decodon strand.” The cis-Decodon strand comprises any number of nucleic acids in length described herein with respect to Decodon elements and can be a unique, specific, single or double strand nucleic acid sequence(s) selected from at least one nucleic acid type or a mixture of nucleic acids including, but not limited to, a Deoxyribonucleic Acid (DNA), Ribonucleic Acid (RNA), Locked Nucleic Acid (LNA), Peptide Nucleic Acid (PNA), Threose Nucleic Acid (TNA), Glycol Nucleic Acid (GNA), 1,5-Anhydrohexitol nucleic acid (HNA), Cyclohexene nucleic acid (CeNA), and Fluoroarabino nucleic acid (FANA) base(s) and / or sequences. The cis-Decodon strand and / or the transDecodon strand, either as a single strand or as part of a double-stranded Decodon strand sequence when paired with its complementary cis-Decodon single strand, provides the unique, identifying nucleic acid sequence for each of the cognate specific amino acids bound specifically by the Ligamer element’s specific amino acid recognition portion.[000166] The phrase “cognate binding element” as used herein refers to the specific amino acid found in a target “protein molecule” bound by the Ligamer’s “specific amino acid recognition portion.”[000167] The phrase “concatenated Decodon strand “as used herein refers to the ligation of the single or double-stranded Decodon strand(s) to the Decodon strands of other bound Conversomes on the same amino acid sequence of a protein molecule. The concatenated Decodon strands are concatenated or chemically joined to form a pDNA strand.[000168] The term “conversion” as used herein refers to the deriving of the pDNA nucleic acid sequence from the amino acid sequence of the “protein molecule” undergoing detection, identification or other analyses as discussed herein. The deriving of the oligonucleotide nucleic acid sequence from a protein molecule’s amino acid sequence provides a completely novel and full representation of the “protein molecule’s” translated DNA template.[000169] The terms “denature,” “denatured” and “denaturing conditions” as used herein refer to the conditions a protein molecule is exposed to that unwind and unfold the tertiary structure of a ’’Protein molecule.” The denaturing of the protein molecule provides access to amino acids that are not at the surface or exposed when the protein molecule’s confirmation is in its tertiary structure.[000170] The term “detectable unfolded polypeptide sequence” as used herein represents an unfolded polypeptide sequence identifiable / detectable by the amino acid sequence as determined from each corresponding specific Conversomes’ specific DNA nucleic acids within each Decodon.[000171] The terms “detect,” “detecting,” “detection,” and “determine” are used interchangeably and refer to at least one of recognizing, observing, and diagnosing in a sample of a suspected “protein molecule” the presence or absence of a protein. Using the pDNA sequence derived from the mixed plurality of Conversome molecules which were collectively bound to the amino acid sequence of a protein of interest, the derived pDNA sequence can be translated via the pDNA’s nucleic acid sequence into the amino acidsequence string of a corresponding protein, if present, as can be found in a protein database, e.g., Swiss-Prot. In so doing one can establish the identity of the protein recognized by the mixed plurality of Conversome molecules in the sample being analyzed .[000172] The terms “identify,” "identifying, "identification,” and “identity” are used interchangeably and refer to at least one of determining, discovering, discerning, distinguishing, confirming the presence or absence in a sample of a suspected “protein molecule” based on the pDNA sequence’s ability to translate the pDNA nucleic acids in the amino acid sequence string of a protein found in a protein database, e.g., Swiss-Prot, that establishes the protein detected by a mixed plurality of Conversome molecules in a sample.[000173] The term “Ligamer element” as used herein refers to the amino acid recognition portion of the Conversome molecule. Each Ligamer element consists of molecules with high binding propensity and can have specificity for, e.g., to one of the 22 genetically encoded (proteinogenic) amino acids, a non-natural amino acid, non-proteinogenic amino acid, modified amino acid resulting from post-translational modification, occurring in non-ribosomal peptide synthesis, an amino acid that is enzymatically or chemically modified in vitro, or a synthetic amino acid incorporated biosynthetically into proteins during translation. Applicant has found that binding of the Ligamer element’s amino acid recognition portion to its specific cognate amino acid (reciprocal) as part of a Conversome molecule (an amino acid recognition portion) provides a method for the discovery, detection, quantitation, and identification of a protein(s) as well as to discover new positions of modification within a protein without the need for instrumentation. The word “Ligamer” is a neologism derived from the Latin ‘ligare’ for “Bind” and ‘ligamen’ for binding and the Greek ‘pepo^’ for ‘meros’ meaning a part or component of a larger target [molecule],[000174] The term “Linker” as used herein is the agent connecting the Decodon element to the Ligamer element of a Conversome molecule. The Linker agent can be any one of, among others: Ethylene glycol, Polyethylene glycol (PEG), Glycerol, Aminopurine, Carbon spacer, Hexanediol, Dideoxyribose, a PC (Photo-Cleavable) Spacer, Melamine, Phenolic and Dialdehydes, Poly(N-(2-hydroxypropyl)methacrylamide, Alpha-D-Glucose, G1 PAMAM dendrimer, sulfonic acid group, glutathione, Poly-L-glutamic acid, and urethane.[000175] The phrase “mixture of proteins” as used herein refers to different protein types (also isoforms) from the same sample at the same time point (Figure 17, Time point 1), or different time points, separate samples of the same cell, tissue, organ or organism without treatment (Fig. 17, Time point 2) or after treatment (Fig. 17, Time point3). The sample can be obtained from a cell, tissue, organ or organism, from one or more organisms, organ, tissue and cell sample. The types of proteins in the sample can be a mixture selected from two or more of enzymes, structural proteins, cell signaling proteins, extracellular proteins, signal transduction proteins, receptor proteins, membrane proteins, transmembrane proteins, antibodies, ligand transport proteins, Lectins, fibrous proteins, and hormones.[000176] The term “modified amino acid” and “modification” are used interchangeably and as used herein refers to an amino acid that has undergone post-translational modification or resulting from non-ribosomal peptide synthesis. The modification can be by phosphorylation, acetylation, N-linked glycosylation, Amidation, hydroxylation, methylation, O-linked glycosylation, Ubiquitylation, Pyrrolidone carboxylic acid, and Sulfation.[000177] The term “modified amino acid specific Conversome molecule” as used herein refers to a Conversome’s Ligamer element which recognizes a “modified amino acid” and a Decodon element comprising at least one specific oligonucleotide nucleic acid sequence strand for each of at least one of a non-natural amino acid, non-proteinogenic amino acid, modified amino acid resulting from post-translational modification, occurring in non-ribosomal peptide synthesis, ora synthetic amino acid. The Decodon element will consist of at least one DNA oligonucleotide nucleic acid sequence strand(s) specific for one of a non-natural, non-proteinogenic amino acid, modified or synthetic amino acid and the DNA oligonucleotide nucleic acid sequence strand is not congruent with the genetic code for the organism.[000178] The phrase “non-specific Conversome molecule” as used herein refers to a Conversome molecule with a universal amino acid identifying Decodon element and a Ligamer element that can bind indiscriminately to any amino acid. The amino acid may not have been bound by its specific Conversome molecule or lacks a specific Conversome molecule, because it is a modified, non-proteinogenic or synthetic amino acid. The non-specific Conversome molecule can also fill in gaps between proteinogenic amino acids both bound and unbound which are bound by their specific Conversome molecule.[000179] The terms “OligoConversomes (molecule),” “pre-linked OligoConversome(s) (molecules)” and “OligoConversome molecule(s)” are used interchangeably and as used herein can refer to two or more either identical or different, specific Conversome molecules’ Decodon elements (FIG. 4A, (412) and (413) with either identical or different, specific oligonucleotide nucleic acid sequences being pre-linked together by concatenation / ligation (FIG. 4A, (402) and (403), respectively) forming OligoConversome molecules with either concatenated double-stranded trans-OligoDecodon strands but not the cis-OligoDecodon strands or concatenated doublestranded cis- and trans-OligoDecodon strands within the respective "OligoDecodon elements” (FIG. 4A, (412) and (413) prior to binding to a target “protein molecule” (401)). Following the pre-linking and binding of the OligoConversomes to their target “protein molecule” the two or more pre-linked Decodon elements (FIG. 4B, (402) and (403)) undergo concatenation (420) by a ligase (230) (FIG. 4G) to other Conversome molecules bound in an interlocking spatial arrangement. A pDNA sequence strand (430) is formed following denaturing of the concatenated trans-Decodon strands releasing the concatenated trans-Decodon strand (430), pDNA sequence strand, for use in detection and / or identification of the target “protein molecule” as illustrated in FIG. 4D. The OligoDecodon pDNA sequence strand oligonucleotide represents the conversion of a “protein molecule” (401) into a pDNA sequence strand (430) between the OligoConversomes (FIG. 4A, (412) and (413)).[000180] The phrase “OligoConversome molecules” as used herein refers to the pre-linking, by use of a ligation reagent or chemical, of at least two or more identical and / or different, specific OligoConversome molecules to form a bi-, tri-, quad-, penta-, hexa-, to deca- or more Multi- Conversomes. The order of the pre-linking of the OligoConversome molecules is determined from the known amino acid sequence of the “protein molecule” to undergo conversion to an OligopDNA sequence.[000181] The phrases “OligoDecodon strand(s)” and “OligoDecodon oligonucleotide nucleic acid sequence strand(s)” are used interchangeably and can refer to Decodons which are pre-concatenated / pre-linked and used as either: i) prior to recognition and binding of Conversomes to a protein element(s) such as a cognate amino acid. In this case Conversomes with a cis-Decodon could bind to cognate amino acids and OligoDecodon strands could be added and bind to the correct Conversomes in the correct order (Fig 11C) or, ii) when there are multiple Ligamers in a Conversome molecule linked by the OligoDecodon strand. (Fig 16A, (1606)). The OligoDecodon strand can be separated from the linker and / or the cis-Decodon strand to form a pDNA nucleic acid sequence strand ready for use in protein analyses processes.[000182] The terms “pDNA” and “pRNA” as used herein represent the single or double-stranded nucleic acid sequence strand(s) formed following concatenation and ligation of several Conversome molecules’ respective Decodon elements’ Decodon oligonucleotide DNA or RNA nucleic acid sequence strand(s). Concatenation can be before binding of the Conversome molecules’ Ligamer elements to each element’s specific cognate amino acid(s) termed “Pre-linked Conversome molecules” or “OligoConversome molecules” or after binding each element to its specific cognate amino acid(s).[000183] The terms “peptide,” “polypeptide,” “protein.”and“proteome” as used herein refer to: i) short amino acid chains (peptides), ii) a much longer contiguous and an unbranched chain of amino acids termed a “polypeptide,” (greater than 50 or more amino acids), iii) polypeptides having a 10,000 dalton (Da) or greater molecular mass termed “proteins,” and iv) a proteome representing the full complement of expressed proteins and proteins that can be expressed by a genome, organism, tissue or cell under defined conditions at a given time. The polypeptide and protein shares with the peptide the linking of the amino acids by peptide bonds. Oligopeptides are amino acid chains of fewer than 20-30 amino acids, examples of which are tripeptides (three peptides), octapeptides (eight peptides) and decapeptides (ten peptides).[000184] The phrases “plurality of different, specific Conversome(s),” “mixture of a plurality of Conversome(s),” and “plurality of a mixture of Conversome(s) molecules” are used interchangeably and herein refer to both several (plurality) different Conversomes molecules each having its own identical Decodon element(s) / Ligamer element(s) simultaneously present as a mixture of different, specific Conversomes for use in a process including, but not limited to, converting a “protein molecule” to a pDNA sequence strand for use to detect and / or identify at least one protein molecule(s) of interest, and / or changes in abundance, conformation / structure, and amino acid mutations or modifications in and as an archival record of the one or more proteins present in a sample to be analyzed. The sample can be obtained from a cell, tissue, organ or organism. The types of proteins in the sample can be a mixture selected from two or more of enzymes, structural proteins, cell signaling proteins, extracellular proteins, signal transduction proteins, receptor proteins, membrane proteins, transmembrane proteins, antibodies, ligand transport proteins, Lectins, fibrous proteins, and hormones.[000185] The phrase “protein in a natural state” as used herein refers to the protein as translated from its genetic code with or without post-translational modification to produce a normal functioning protein. The protein could also be present in its naturally folded / native conformation depending on this function.[000186] The term “pre-link” as used herein refers to the concatenation of a first Conversome molecule’s Decodon strand to a second Conversome molecule’s Decodon strand prior to the addition of a mixture of a plurality of Conversome molecules to a solution containing a protein molecule(s) of interest. The pre-linking can be between two or more Conversome molecules’ cis-Decodon strands, double-stranded Decodon strands’ transDecodon strands and double-stranded Decodon strands’ both cis-Decodon and its complementary trans-Decodon strands oligonucleotide nucleic acid sequences. Pre-linkingcan also occur using a string of nuclei acids to pre-link Ligamer elements by the Linker element of each.[000187] The phrase “protein molecule” as used herein collectively refers to all or any one of a “peptide,” “polypeptide,” “protein,” and “proteome” that can be converted into a pDNA sequence using a mixture of a plurality of Conversome molecules for detection and identification of a plurality of amino acids, as they exist, in a sample to be analyzed, as an amino acid sequence within the ‘protein molecule of interest.’[000188] The phrase “protein recognition molecule” as used herein refers to the Conversome molecule as illustrated in Figures 1A and 1B.[000189] The phrase “Proteome modification” as used herein can refer to the post-translational modification of the cell, tissue or organism by one or more of phosphorylation, acetylation, N-linked glycosylation, Amidation, hydroxylation, methylation, O-linked glycosylation, Ubiquitylation, Pyrrolidone carboxylic acid, and Sulfation. (Swiss-Prot database, Khoury GA, Baliban RC, Floudas CA (September 2011). "Proteome-wide post-translational modification statistics: frequency analysis and curation of the Swiss-Prot database". Scientific Reports 1(90):90. Bibcode: 2011NatSR...1E..90K. doi:10.1038 / srep00090. PMC 3201773. PMID 22034591.[000190] The phrase “unfolded polypeptide sequence(s)” as used herein refers to the denaturing of a peptide, polypeptide, or protein sequence. This can result in greater accessibility to the amino acids that form the peptide, polypeptide, or protein sequence. Denaturation can be accomplished by applying heat to the solution containing the protein molecule(s) of interest, use of or addition of chemical(s) as well as rigidifying the backbone of proteins and polypeptides to be analyzed.[000191] The phrase “detectable, unfolded polypeptide sequence" as used herein represents an unfolded polypeptide sequence identifiable / detectable by the amino acid sequence as determined from each corresponding specific Conversomes’ specific nucleic acid within each Decodon and from the same unfolded polypeptide sequence that were concatenated together to form a strand specific oligonucleotide sequence (pDNA) representing each unfolded polypeptide sequence(s).[000192] The phrase “post-translational modification” as used herein can refer to the changing of proteins by a covalent process following protein synthesis. This can include, but is not limited to, an amino acid(s) modification including, but not limited to, phosphorylation, acetylation, N-linked glycosylation, Amidation, hydroxylation, methylation, O-linked glycosylation, Ubiquitylation, Pyrrolidone carboxylic acid, and Sulfation. Protein modifications can also occur at the C- or N- termini, formation of disulfide bonds, cleavingpeptide bonds, oxidative stress, chemical modification of amino acids, structural changes and the like as is known to one of skill in the art.[000193] The phrase “two or more different, unfolded polypeptide sequences” as used herein can refer to the presence in a “protein molecule” of interest unfolded (denatured) “protein molecules.”[000194] The term “Pre-linked Conversome molecules” as used herein refers a plurality of DNA oligonucleotide nucleic acid sequence strands from more than one Conversome molecule’s Decodon element concatenated together prior to the binding of each Conversome’s “Ligamer element’s” specific amino acid recognition portion which binds to its specific, cognate amino acid element. It is anticipated that the amino acids for each of the Conversomes are either adjacent, consecutive or in a suitable spatial arrangement to allow concatenation on the amino acid sequence of the target peptide, polypeptide, protein or proteome.[000195] The term “Protein sequence” as used herein refers to nitrogenous organic compounds having large molecules of one or more long chains of amino acid sequence(s) which forms a protein molecule.[000196] The term “Proteinogenic amino acid” as used herein refers to the 20 genetically encoded amino acids found in the standard genetic code that are used in the biosynthesis of proteins during translation plus two additional amino acids, selenocysteine and pyrrolysine, who can be incorporated into protein(s) using special translation mechanisms.[000197] The term “non-proteinogenic amino acid” as used herein refers to amino acids either incorrectly incorporated into a protein in place of a genetically encoded amino acid, not biosynthesized by the cell’s standard mechanisms, or not incorporated into proteins.[000198] The phrase “pseudo-OligoConversome” as used herein refers to the pre-linking of Ligamer elements but lacking Decodon Elements which are used for detection of specific amino acid sequences in a target protein. Single-stranded nucleic acids or other types of chemical linkages (1000) are attached to and pre-link each of a first end of two or more Linker elements whose opposite, second ends are each attached to at least one Ligamer amino acid recognition portion(s) creating pre-linked Ligamer elements. The single-stranded nucleic acids or other types of chemical linkages (1000) pre-linking the Ligamer elements can have a Detection molecule (901) at one end of the single-stranded nucleic acids or other types of chemical linkages (1000). Different pseudo-OligoConversome(s) with pre-linked single-stranded nucleic acid strands connected toeach Linker element connected to its targeted Ligamer element targeted for pre-linking are added to the target protein sample in solution and then the Ligamers bind to their targeted cognate amino acids within the target protein as illustrated in Fig. 10. Detecting the target protein sequence can then be done via the pre-linked Ligamers (1000) which are connected to a fluorescent molecule or via an enriched immunoprecipitation assay via a linked bead (901).[000199] The phrase “specific protein” as used herein refers to a “protein molecule” with at least one of: a known amino acid sequence, a known function, a known modification(s) or mutation(s). In terms of a “Conversome molecule” the Decodon strand and its corresponding Ligamer portion are unique to a single or multiple, specific amino acid(s) based on the Ligamer element’s amino acid recognition portion. If there are two or more amino acid recognition portion(s) associated with one Ligamer element, then the specific Decodon strand’s nucleic acid sequence is unique to the two or more amino acid recognition portion(s) associated with the one Ligamer element of the specific Conversome molecule. The type of cognate amino acid(s) recognized by the Ligamer element can be any one of a proteinogenic, non-proteinogenic, modified or synthetic amino acid. Fig. 16A illustrates two Decodon strands (1606) and (1608) unique to two adjacent amino acids on the unfolded protein strand (401) and these two amino acid recognition portions are specific to the protein encoded by the unfolded protein strand (401). The specificity of the amino acid sequence that makes up a specific protein also provides the specific protein with the specificity necessary to perform its specific function or not function.[000200] The phrase “splint oligonucleotide" as used herein refers to a DNA or RNA nucleic acid molecule which hybridizes and binds to a complementary specific sequence which is made of any number of nucleic acids in length described herein with respect to Decodon elements. The splint oligonucleotide binds the complementary molecules that are directly adjacent to one another or are in an interlocking spatial arrangement to one another. The complementary strands hybridized by the splint oligonucleotide, the bound strands, are the Conversome molecule’s cis-Decodon strands. In this application a concatenation agent then concatenates the hybridized cis-Decodon strands to create a pDNA sequence strand composed of cis-Decodons. This process is similar to the sealing of a nick in a genome (Chao J et al (2015). Configuration Transitions of Free Circular DNA System Induced by Nicks. J of Nanomaterials. 2015: 546851) and is more efficient than a double-stranded concatenation because the 5' phosphate and 3' OH substrates are positionally stabilized by the splint oligonucleotide.[000201] The phrases “strand specific oligonucleotide nucleic acid sequence (pDNA or pRNA),” “specific oligonucleotide nucleic acid sequence strand,” and “pDNA orpRNA” are used interchangeably and refer to the concatenated DNA or RNA oligonucleotide nucleic acid sequence strands from within the Decodon element(s) of each of the corresponding amino acid specific Conversomes’ amino acid recognition portion, the Ligamer element, bound to a target “protein molecule” (a peptide, polypeptide, protein or proteome). The formation of each specific oligonucleotide pDNA sequence strand represents a detectable polypeptide sequence and the pDNA can be used in qPCR, Next Generation Sequencing (NGS), nanopore sequencing, digital PCR, Sanger Sequencing or other nucleic acid analysis method familiar to one skilled in the art.[000202] The term "substantially" as used herein refers to a majority of, or mostly, as in at least about 50%, 60%, 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99%, 99.5%, 99.9%, 99.99%, or at least about 99.999% or more.[000203] The phrase “synthetic amino acid” and “unnatural amino acids” can be used interchangeably and as used herein refers to an amino acid that is not part of the genetic code, not found in nature and exists due to being synthesized chemically in a laboratory.[000204] The phrase “targeted conversion” as used here can refer to the prelinking of two or more specific Conversomes’ Decodon Elements’ oligonucleotide nucleic acid sequence(s). The specific Conversomes are selected for each Conversome’s specific amino acid recognition portion and the order of concatenation of the Decodon Elements is predicated on the knowledge of the order of the amino acids in a target “protein molecule(s)” as illustrated in FIGs 4A-4D).[000205] The term “treating” as used herein refers to the administration of a therapeutic agent to alleviate symptoms, eradicate an infection or inflammation or cure a disease to a patient in need thereof.[000206] The term “Unmodified amino acid” as used herein refers to an amino acid that does not have a covalently attached methyl, Phosphate, Ubiquitin (or other) molecule. The amino acid is in its native / natural state.DETAILED DESCRIPTION[000207] Disclosed herein are embodiments for producing the DNA sequence, termed pDNA for “DNA derived from a protein,” from any one of a peptide, polypeptide, protein and proteome, collectively herein referred to as a “protein molecule,” by identifying the amino acid sequence(s) of the protein molecule(s). The ability to obtain the DNA sequence of the protein molecule’s amino acid sequence is attributed to the development of a novel protein recognition molecule. The protein recognition molecule can separately, at the binding endof the protein recognition molecule, bind to its specific cognate amino acid(s) and so detect and / or identify each amino acid or adjacent amino acids within the amino acid sequence. The protein recognition molecule in concert with adjacent protein recognition molecules also bound to their respective amino acid(s) in the amino acid sequence, are concatenated together at the opposite end of the binding end and can produce the pDNA sequence from the sequence of amino acids in the amino acid sequence bound by the mixture of a plurality of novel protein recognition molecules, the Conversome™ molecules as illustrated in Figures 1 A and 1 B. Figures 1 A-1 B illustrates the conversion of a protein to pDNA which begins with a protein recognition molecule, a Conversome™ molecule developed by Applicant to both recognize and bind to its cognate / reci procal, specific amino acid found in the amino acid sequence of the protein molecule, but also associates a unique oligonucleotide nucleic acid strand to the specific cognate amino acid.[000208] The Conversome molecule (Fig. 1A (100), Fig. 1B (110), comprises a first end, a Decodon element (Fig. 1A, (103)) containing at least one of i) a first, specific oligonucleotide nucleic acid sequence strand of one single strand cis-Decodon strand (104), and / or a second, specific oligonucleotide nucleic acid sequence strand of one single strand trans-Decodon strand (not shown). The Decodon element (Fig. 1B, (106) can comprise either a single-stranded Decodon strand (cis- or trans-Decodon strand) or a specific oligonucleotide nucleic acid sequence double strand of one cis-Decodon strand (104) paired with its complementary trans-Decodon strand (105). Assembly of the Conversome molecule is presented in Example I.[000209] The nucleic acids comprising the Decodon’s oligonucleotide nucleic acid sequence strand(s) are selected from at least one or more nucleic acids selected from the group comprising, but not limited to, a Deoxyribonucleic Acid (DNA), Ribonucleic Acid (RNA), Locked Nucleic Acid (LNA) Peptide Nucleic Acid (PNA), Threose Nucleic Acid (TNA), Glycol Nucleic Acid (GNA), 1,5-Anhydrohexitol nucleic acid (HNA), Cyclohexene nucleic acid (CeNA), and Fluoroarabino nucleic acid (FANA) base(s) and / or sequences.[000210] Opposite the first end Decodon element is a second end comprising a Ligamer element (101) comprising at least one amino acid recognition portion (102). The amino acid recognition portion has a strong propensity and specificity for the Conversome molecule’s specific amino acid. The Ligamer’s amino acid recognition portion will bind to the Conversome molecule’s cognate amino acid within the protein molecule’s amino acid sequence.[000211] The Decodon element and Ligamer element are connected via a Linker element (108). The Linker element binds to both the Decodon element to at least one nucleic acid of the cis-Decodon strand and to the Ligamer element’s amino acidrecognition portion. Moreover, the Ligamer element can comprise at least a second specific amino acid recognition portion for binding to a second specific amino acid within the amino acid sequence of the protein molecule and the first and second specific amino acid recognition portions can bind to adjacent first and second specific amino acids within the amino acid sequence of the protein molecule. The linker is selected from the group consisting of Ethylene glycol, Polyethylene glycol (PEG), Glycerol, Aminopurine, Carbon spacer, Hexanediol, Dideoxyribose, a PC (Photo-Cleavable) Spacer, Melamine, Phenolic and Dialdehydes, Poly(N-(2-hydroxypropyl)methacrylamide, Alpha-D-Glucose, G1 PAMAM dendrimer, sulfonic acid group, glutathione, Poly-L-glutamic acid, and urethane.[000212] When a mixture of a plurality of the Conversome molecule’s Ligamer elements specific amino acid recognition portion(s) are bound to their respective cognate amino acid(s), of the protein molecule’s amino acid strand, one can detect(s) and / or identify(s) the protein molecule(s). Detection or identification is based on each Decodon element’s first, and / or second oligonucleotide nucleic acid strand(s) when concatenated together with other Decodon element’s first and / or second oligonucleotide nucleic acid strand(s), on the same amino acid sequence strand, to form a pDNA sequence(s) strand for each of the one or more protein molecules in a protein sample to be analyzed.[000213] The protein molecule’s amino acid sequence will comprise any one of a proteinogenic, non-proteinogenic, modified and synthetic amino acid. As is known to the skilled artisan, amino acids can be inaccessible when a protein molecule is in its natural state. The ability of the Conversome molecule to specifically recognize each amino acid with specificity relies on the amino acid to be accessible. Accessibility can be aided by denaturing the protein in a suitable solution to unfold the protein of interest, rendering greater access to the amino acids by their cognate Conversome molecules. An example of a suitable protein detection / identification and target protein denaturation solution is a solution of 10mM Tris pH 8.0, 0.1% TritonX 100, 5mM MgCI2, and 50mM KCI.Denaturation can also be accomplished by applying heat to the solution containing the protein molecule(s) of interest, use of or addition of chemical(s) as well as rigidifying the backbone of proteins and polypeptides to be analyzed.[000214] The polypeptide / protein backbone may be modified to maintain rigidity, or to go inside out. This can entail at least one of protein denaturation or stiffening; however, the latter can have conformational restrictions. Furthermore, detergents may be incorporated to make sure proteins don’t crash out of solution. Suggested detergents include, but are not limited to: Triton X100, Tween 20, Tween 80, cetyl trimethylammonium bromide (CTAB), BRIJ™-35, (30% (w / w) Solution (Thermo Scientific, a nonionic polyoxyethylene surfactant (15.0g Brij 35 (polyoxyethylene auryl ether, AtlasChemid, BDH, or equivalent) dissolved in about 70 ml deionized water with heating to 60°C to aid dissolving, cool and bring to 100-ml in a volumetric flask with deionized water), used in cell lysis buffers or in various HPLC applications as a surfactant), NP-40 alternative (CAS 9016-45-9, Nonylphenyl Polyethylene glycol, Millipore Sigma), and CHAPS (3-[(3-Cholamidopropyl) dimethylammonio]-1-propanesulfonate), a sulfobetaine derivative of cholic acid and a zwitterionic detergent used to maintain protein activity when membrane proteins are solubilized.[000215] One alteration of the protein’s confirmation can be causing the backbone of the protein’s three dimensional structure to form a helix with amino acids, on the outside of the protein’s confirmational structure, in order to facilitate accessibility to the amino acids and so allow a mixture of a plurality of Conversome molecules to bind to each Conversome’s specific cognate amino acid.[000216] The polypeptide backbone that comprises the core of proteins and other polypeptides allows for substantial conformational flexibility in the molecules, which can have a noted effect on the molecules’ three dimensional shape. Conformational restriction can be accomplished via chemical means. For example, an a-helical conformation can be stabilized by covalent cross-links between the side chains of amino acid residues that are separated by one, two, or three turns. A convenient way to achieve these cross-links is by incorporating unnatural amino acid side chains with appropriate spacing in the polypeptide. When the unnatural amino acid side chains involve terminal olefins, a ring closing metathesis reaction can be used to join the olefin termini, resulting in a “staple” in the a-helix that greatly increases the polypeptide’s chemical and thermal stability, protease resistance, and amino acid accessibility by a mixture of a plurality of specific Conversome molecules. For a representative reference, see Kim et al., Organic Letters 2010, 12(13): 3046-3049.[000217] Natural amino acids can also be used to provide enhanced conformational rigidity in polypeptides and proteins. Specifically, the naturally occurring amino acid proline is unique in that it contains a cyclic structure that joins its amine and methine carbon atom. Polyproline molecules, i.e. polypeptides which are comprised of multiple proline residues joined together by conventional peptide linkage bonds, possess enhanced conformational rigidity compared with other poly-amino acids. In fact, this rigidity has been used to prepare “molecular rulers” on the atomic scale as these polyproline molecules are recognized as compounds of reliable size and shape that do not change under normal conditions. These relatively rigid proline oligomers can be introduced into proteins of interest by solid phase synthesis, or by genetic expression. For a representative reference, see Moradi et al., PNAS 2009, 106(49): 20746-51.[000218] The protein(s) molecule(s) for analysis by Conversomnique™ methods can be any one of a mixture of proteins wherein the protein(s) are mixture of two or more proteins to be identified and / or detected. Moreover, the first, specific, reciprocal / cognate, amino acid within the protein(s) bound by the Ligamer’s first, specific amino acid recognition portion can be any one of the twenty-two proteinogenic amino acids.[000219] Table 1: Proteinogenic Amino Acids00220] L-Alanine [000221] L-Arginine 222] L-Asparagine 300223] L-Aspartic acid 0 KIN Q Q oH3C^ A 1. Z .-x A OH A’■f y ’CHaY.y OHNH; T OH T 'OHNH2>0224] L-Cysteine 000225] L-Glutamic [000226] Glycine 100227] L-Histidine acidp o o1 . 4 ^-.oH<y Y ■'■QH H2N Y A OH / -AHH / HjH' V ^ .06H228] L-lsoleucine [000229] L-Leucine [000230] L-Lysine )231] L-Methionine 0Y OH I.‘z" Tw,s., -. AHsC y QH T 1 '”[000232] L- [000233] L-Proline [000234] L-Serine 0235] L-Threonine Phenylalanine0 0 OH O... JIfi 'T rw / ''Y' '''O HQ- Y AHOMNH2YX"°H NH2[000236] L- [000237] L-Tyrosine [000238] L-Valine [000239] L- Tryptophan SelenocysteineCT YwXJH A -OHHX Y H2N' y6 6[000240] L- Pyrrolysine[000241] Additionally, the first, specific, reciprocal / cognate amino acid within the protein(s) bound by the Ligamer’s first, specific amino acid recognition portion, can also be anyone of a non-proteinogenic, modified or synthetic amino acid.[000242] When constructing the Decodon strands, it can be that the cisDecodon’s first oligonucleotide nucleic acid sequence consists of either a DNA or an RNA nucleic acid(s) sequence. An oligonucleotide nucleic acid sequence strand of one singlestranded cis-Decodon strand can be concatenated to a second oligonucleotide nucleic acid sequence strand of a Decodon. Likewise, a double-stranded oligonucleotide nucleic acid sequence strand comprising a cis-Decodon strand and its complementary trans-Decodon strand can be concatenated to a second double-stranded oligonucleotide nucleic acid sequence strand comprising a cis-Decodon strand and its complementary trans-Decodon strand of an adjacent Decodon strand’s double-stranded oligonucleotide nucleic acid sequence strand in interlocking spatial distance. Concatenation can be chemical concatenation selected from the group consisting of pi (TT) conjugation, sigma (o) conjugation, and hyperconjugation. There can be used in the chemical concatenation either a chemical concatenation agent such as an enzyme selected from the group consisting of T4 DNA Ligase, RtcB Ligase, T3 DNA Ligase, T7 DNA ligase, E. coli DNA Ligase, SplintR Ligase, TaqDNA Ligase, 9°N DNA Ligase, T4 RNA Ligase 1, T4 RNA Ligase 2, Aminoacyl tRNA synthetase, Succinyl coenzyme A synthetase, Thiokinase, Ubiquitin Ligase, argininosuccinate synthetase, Gamma-glutamyl carboxylase, Polyketide synthase, DNA Ligase, Chelatases, Glutamate-cysteine ligase, and / or a the chemical process selected from Click Chemistry, reductive amination, and phosphoramidite chemistry.[000243] The Decodon’s double-stranded specific oligonucleotide nucleic acid sequence strands’ ends can comprise one or more sequence end configurations selected from: blunt ends, a 1 base 5’ overhang, 2 bases 5’ overhang, 3 bases 5’ overhang, 1 base 3’ overhang, 2 bases 3’ overhang, or 3 bases 3’ overhang nucleic acid ends. These ends are useful for directing concatenation in a specific order of Conversome molecule’s Ligamer element’s amino acid recognition portions when pre-linking Decodon strands or adding a capture moiety or peptide molecule to verify a protein molecule’s presences or identity within a protein sample being analyzed.[000244] The Decodon elements with double-stranded oligonucleotide nucleic acid sequences can comprise various end types as illustrated in Figs. 15A and 15B. The end configurations can comprise at least one strand with a blocked end, (1500) or a Hydrogen (H) on the 5’ end (1510) or on the 3’ end (1520) of a DNA, RNA or other nucleic acid type, which does not provide the functional groups for concatenation. Both strands blocked with a H on the same end of each of the two strands (1510 and 1520); both strands with blocked ends (not shown); and H at both ends of one strand, (1540 and 1530), wherein the strand(s) with the blocked end or the end(s) 5’ PC or 3’ OH are replaced by H are precluded from concatenation with adjacent or proximal Conversomes’ Decodon elements’ single or double strand oligonucleotide nucleic acid sequence(s).[000245] In another embodiment, two or more different and / or identical amino acid specific Conversome molecules’ Decodon elements’ double-stranded nucleic acid Decodon strands can be pre-linked to one another (termed an OligoDecodon element) to form an OligoConversome with double -stranded nucleic acid OligoDecodons prior to addition of a mixture of a plurality of different, specific Conversome molecules to a solution of at least one protein to be detected. The two or more Conversome molecules’ OligoDecodon elements can be pre-linked through at least one of the trans-Decodon strands, cis-Decodon strands, or both cis- and trans-Decodon strands.[000246] Figure 4 depicts a form of targeted conversion of a targeted protein.[000247] To illustrate, Figs. 4A-4D depict formation of OligoConversome molecules (412) and (413) from three different specific Conversome molecules’ double strand Decodon strands concatenated by the trans-Decodon strands ((402) and (403), Fig.4A) in each of three different, specific Conversome molecules.[000248] Figure 4A depicts addition of a pair of pre-linked OligoConversomes each with three Conversome molecules with double-stranded DNA OligoDecodons (prelinked oligonucleotide nucleic acid sequences, 412 and 413) to a solution containing the denatured protein.[000249] Following addition of the OligoConversome molecules to a solution containing a denatured protein to be detected the OligoConversome molecules bind to their cognate amino acids (FIG. 4B). A single concatenation reaction between pre-linked double strand Decodon strands (402) and (403) forms a single oligonucleotide nucleic acid sequence, the OligoDecodon pDNA sequence (Fig. 4C, (420)). The OligoDecodon is released from the cis-Decodon and available for qPCR or other methods known to the skilled artisan for protein detection using the pDNA sequence (Fig. 4D, (430)) derived from the unfolded protein’s amino acid sequence. The release of the pDNA sequence strand(430) can be accomplished by the following methods including, but not limited to, denaturation using heat, degradation of the cis strand, cleavage of the Linker element, denaturation using high salt, and sodium hydroxide. The OligoConversome molecules can be bi-, tri-, quad-, penta-, hexa-, to deca- or more pre-linked Conversome molecules to form Multi-OligoConversome molecules.[000250] In some aspects the Conversome molecule(s) provide a method for using DNA to detect a protein as illustrated in Figures 2A-2G. Proteins are normally in a somewhat ordered, folded structure that can be described as a three-dimensional structure, native state and tertiary confirmation. The folding contributes to the protein’s biological functioning. In the disclosed innovation, protein detection and determination of a protein’s DNA sequence based on the protein’s amino acid sequence begins with the unfolding via denaturation of the protein to permit access to the amino acids as depicted in Fig. 2A.[000251] Figure 2A depicts, in a sample, one of a plurality of unfolded polypeptide sequences (200) following denaturation of at least one specific protein within a mixture of proteins to be detected ((201), target protein). Alternatively, a protein could be locked into a confirmation that allows amino acid access to perform the detection reaction. For example an a-helix induced into the 3-D structure, as a lock, which puts most amino acid side chains on the outside (surface of the protein, and so accessible, not shown).[000252] Following restructuring of the protein, by denaturation, for greater amino acid accessibility a mixture of a plurality of different, specific Conversome molecules is added to the solution of the unfolded polypeptide sequence(s) of FIG. 2A. Each specific Conversome molecule will bind to its corresponding cognate amino acid within the unfolded polypeptide sequences(s) as illustrated in Fig. 2C followed by the concatenation and ligation (230) of one strand (trans- Decodon strand) for each of the specific Decodon double-stranded DNA nucleic acid strand(s) from each Conversome molecule’s Decodon element of FIG. 2C, creating a pDNA (240) as depicted in Figures. 2D-2F.[000253] Figure 2G depicts denaturation of the concatenated DNA strand(s) releasing the concatenated DNA sequence (242) from the Decodon double-stranded DNA nucleic acid strand sequences and enabling detection of the concatenated DNA sequence derived from the target protein.[000254] In some embodiments, envisioned are still other methods for detection of a protein by DNA sequence. Figures 3A-3E illustrates variations on the detection method of Figures 2A-2G. For example, both the cis-Decodon and trans-Decodon double-stranded DNA nucleic acid strand sequences can undergo concatenation and ligation as illustrated in Fig. 3A as compared to Figs 2D-2F.[000255] In yet more embodiments, Fig. 3B illustrates ligation of specific, Conversome molecules having a single-stranded Decodon DNA nucleic acid strand (or Decodon RNA nucleic acid strand). Applicant notes that alternative nucleic acids can be inserted into a DNA or RNA oligonucleotide nucleic acid Decodon strand including, but not limited to Locked Nucleic Acid (LNA) Peptide Nucleic Acid (PNA), Threose Nucleic Acid (TNA), Glycol Nucleic Acid (GNA), 1,5-Anhydrohexitol nucleic acid (HNA), Cyclohexene nucleic acid (CeNA), and Fluoroarabino nucleic acid (FANA) base(s) and / or sequences. Following concatenation the concatenated sequence(s) can be released from the bound Conversomes by cleavage of the linkers (340) joining the Decodon to their Ligamer thereby releasing the concatenated single-stranded Decodon DNA nucleic acid strands and concatenated pDNA (302) to be detected as illustrated in Fig. 3C compared to denaturation in Fig. 2G. Alternatively, use of Decodon double strand Decodon RNA nucleic acid strand, as the cis-Decodon, can, following concatenation, be subsequently degraded with a nuclease or with heating and divalent cation to release the pDNA (242) for detection as illustrated in Fig. 3D versus denaturation in Fig. 2G.[000256] The chemical concatenation of Decodons strands (360) instead of an external factor (230) such as “a ligase” can also produce the pDNA sequence strand as illustrated in Fig. 3E.[000257] In another aspect, disclosed are processes for detecting the presence or absence of at least one specific protein, a mixture of proteins, or distinguishing between two or more different proteins in a sample with the disclosed Conversome molecules supra. The sample is suspected of containing said protein or proteins. The various steps to detect the protein(s) starts with treating the sample under denaturing conditions. This treatment will unfold at least one specific protein, the mixture of proteins or the two or more different proteins to be distinguished in the sample. The sample can have unfolded protein(s) / polypeptide(s), a mixture of unfolded polypeptides or two or more different, unfolded polypeptide sequences. To the unfolded polypeptide(s) is added a mixture of a plurality of different, amino acid specific Conversome molecules. Each Conversome molecule’s Ligamer’s specific amino acid recognition portion will in turn bind to its corresponding cognate, specific amino acid within the unfolded polypeptide sequence(s) amino acid sequence(s).[000258] The process of detecting the protein(s) proceeds with treating the plurality of bound Conversome molecules’ first ends, the Decodon elements, comprising either: one single strand (cis-Decodon) of a first oligonucleotide nucleic acid sequencestrand, one single strand (trans- Decodon) of a second oligonucleotide nucleic acid sequence strand or one double-stranded (cis-Decodon paired with its complementary trans-Decodon) of a third oligonucleotide nucleic acid sequence double strand with a concatenating agent; wherein each Conversome’s Decodon element’s oligonucleotide nucleic acid sequence strand(s), either the single cis-Decodon or trans-Decodon strand sequences or the double cis- trans-Decodon strand sequences are concatenated together to form a strand specific oligonucleotide nucleic acid sequence(s) (termed a concatenated pDNA oligonucleotide nucleic acid sequence(s) or concatenated pRNA nucleic acid sequence(s)) each pDNA oligonucleotide nucleic acid sequence represents the amino acid sequence of a detectable polypeptide sequence(s). The pDNA oligonucleotide nucleic acid sequence will be separated from the Conversomes bound to the amino acid sequence of the unfolded protein(s) by treating the pDNA oligonucleotide nucleic acid sequence(s) as described in Figures 2 and 3 supra to isolate the concatenated pDNA oligonucleotide nucleic acid sequence(s) for use in detecting and / or identifying the protein sequence(s) in the sample as well as distinguishing between two or more different proteins in said sample or detecting and / or identifying at least one specific protein in the sample containing a mixture of proteins. The pDNA oligonucleotide nucleic acid sequence(s) are detecting and / or identifying at least one specific protein in the sample containing the mixture of proteins or identify or distinguishing between two or more different proteins in the sample.[000259] The oligonucleotide nucleic acid sequence(s) of the cis-Decodon and trans-Decodon comprise at least one more of a nucleic acid selected from the group consisting of: Deoxyribonucleic Acid (DNA), Ribonucleic Acid (RNA), Locked Nucleic Acid (LNA) Peptide Nucleic Acid (PNA), Threose Nucleic Acid (TNA), Glycol Nucleic Acid (GNA), 1,5-Anhydrohexitol nucleic acid (HNA), Cyclohexene nucleic acid (CeNA), and Fluoroarabino nucleic acid (FANA) base(s) and / or sequences.[000260] In some embodiments, targeted conversion can be used to detect a protein molecule by pre-linking at least two or more Conversome molecules’ Decodon element’s oligonucleotide nucleic acid sequences by concatenation prior to binding to the unfolded protein. The order of the Conversomes’ linking together is directional, based on Decodon type (illustrated in Figs. 15A and 15B) and predicated from a known amino acid sequence for a sequenced protein. Any one of the Decodon strands, either the single strand cis-Decodon strand(s), single strand trans-Decodon strand(s) and double-stranded oligonucleotide nucleic acid sequence strands comprising cis-Decodon strands and its complementary trans-Decodon strands can be pre-linked together.[000261] As illustrated in Fig. 4A two sets of three pre-linked OligoConversomes with double-stranded DNA OligoDecodons are pre-linkedoligonucleotide nucleic acid sequences. The trans-Decodon strands are pre-linked to form connected OligoConversome molecules (412) with pre-linked trans-Decodon (402) and connected Conversome molecules (413) with pre-linked trans-Decodon (403). The OligoConversomes (412 and 413) are added to a solution containing the denatured protein (401). Fig. 4B illustrates the binding of each pre-linked OligoConversome from FIG. 4A to its specific cognate amino acid(s)s by each of the corresponding Ligamer’s specific amino acid recognition portion bound to each of their specific, cognate, amino acid, said amino acids occurring as consecutive or in interlocking spatial proximity to amino acids on the unfolded polypeptide sequence(s)within the denatured protein’s sequence (i.e. , (401) a sequence of amino acids) and the cognate amino acids can be any one of a standard, proteinogenic amino acid, a modified amino acid, a non-proteinogenic amino acid and a synthetic amino acid. Fig. 40 shows a single concatenation together, by a ligase (230), of the two pre-linked OligoConversomes’ (412 and 413) double-stranded DNA OligoDecodon oligonucleotide nucleic acid sequences (concatenation of the trans-Decodon sequences) from Figs. 4A-4B into a single oligonucleotide nucleic acid sequence, the OligoDecodon pDNA sequence (420).[000262] Alternatively, a protein molecule’s specific protein sequence can be detected by employing OligoConversomes. At least two or three different, pre-linked Conversome molecules (900) can be concatenated by either one of or both of their respective Decodon elements’ cis- and trans-Decodon strands (e.g., (902) and (904)) and are able to bind to two or three or more adjacent or in interlocking spatial position to amino acids on the unfolded polypeptide sequence(s) (401) and labelled with a fluor or magnetic bead (901) attached to the end of one of the concatenated double-strand pDNA sequence strands. Detection of the unfolded polypeptide sequence can be by fluor or enriched by immunoprecipitation as illustrated in Figs. 9A and 9B.[000263] Figure 9 illustrates detection of specific protein sequences using OligoConversomes.[000264] Figure 9A depicts the use of OligoConversomes (900) linked to a target protein molecule’s unfolded amino acid sequence (401) based on the protein sequence. The Decodon elements’ Decodon strands are pre-linked ((902) and (904)) reserving the amino acid recognition portion of the Ligamer elements for binding to their respective cognate amino acids. Attached to the 5’ end of one of the pre-linked, concatenated Decodon elements trans-Decodon strand is a Detection molecule (901) that could be a fluor, enzyme, a bead with different density, or a magnetic bead (or other affinity reagent) as known to one of skill in the art for protein detection.[000265] Figure 9B illustrates detection of a specific protein sequence following binding of the linked Conversomes and the protein sequence is detected.[000266] Alternatively, a pseudo-OligoConversome can be used to take advantage of targeted amino acid recognition portions pre-linked by a single-stranded nucleic acid strand (1000) (similar to a single strand cis-Decodons) for detection of specific amino acid sequences in a target protein (401). Different pseudo-OligoConversome with pre-linked single-stranded nucleic acid strands connected to each Linker connected to its targeted Ligamer element targeted for pre-linking are added to the target protein sample in solution and then the Ligamers bind to their targeted cognate amino acids within the target protein as illustrated in Fig. 10.[000267] The pDNA sequence is released from the Conversome molecules following denaturation. The release from the linker can be by binding RNA to the linker followed by degradation of the RNA with at least one of temperature, divalent captions, RNAse, or nuclease to release the concatenated Decodon strands’ pDNA sequence. The pDNA sequence is specific for one unfolded polypeptide sequence corresponding to one protein that can be detected using the pDNA sequence in a protein detection assay including, but not limited to qPCR, NGS, TaqMan® assay, qRT-PCR, and RNA NGS, as known to the skilled artisan.[000268] In some embodiments, envisioned is a plurality of Conversome molecules having the identical first ends (Decodon elements and Decodon strands) and the identical second ends, non-specific Ligamer elements. Each non-specific amino acid recognition portion of the Ligamer element is able to bind, on the unfolded polypeptide sequence, to any accessible, unbound amino acid(s) including those cognate amino acids not represented by a specific (amino acid) Conversome molecule. The addition of the plurality of non-specific Conversome molecules can follow the addition and binding of the specific Conversome molecules. The use of non-specific Conversome molecules to complete the pDNA sequence by filling in gaps due to either the lack of a proteinogenic Conversome(s) or a Conversome specific for i) an amino acid that is modified, ii) a non-proteinogenic amino acid or possibly iii) a synthetic amino acid. This becomes a process of gap filling on an amino acid sequence of an unfolded protein molecule as illustrated in Figs. 5A-5D.[000269] Often knowing the position of a few (e.g., about 3 to about 4, about 3 to about 5, about 3 to about 6, about 3 to about 7, about 3 to about 8, about 3 to about 9, about 3 to about 10, about 4 to about 5, about 4 to about 6, about 4 to about 7, about 4 to about 8, about 4 to about 9, about 4 to about 10, about 5 to about 6, about 5 to about 7, about 5 to about 8, about 5 to about 9, about 5 to about 10, about 6 to about 7, about 6 toabout 8, about 6 to about 9, about 6 to about 10, about 7 to about 8, about 7 to about 9, about 7 to about 10, about 8 to about 9, about 8 to about 10, or about 9 to about 10) contiguous amino acids within a protein sequence can be adequate for protein sequence detection and / or identification. As shown in Fig. 5A the process begins with the addition of a plurality of specific Conversomes (216, 213, 212) for a subset of amino acids present in the target, unfolded protein (500) in solution. Fig. 5B depicts the specific Conversomes binding to their cognate amino acid(s) on the unfolded protein (500). Fig. 5C illustrates the further addition of identical (a plurality) of non-specific Conversome molecules (501) capable of non-discriminate binding to all unbound / open amino acids awhich thereby “fills in” gaps in the elucidation of the amino acid sequence of the unfolded protein (500) as depicted in Figure 5D. As illustrated in Fig. 5E all of the bound specific and non-specific Ligamers with their respective Conversome’s trans-Decodon strands are concatenated together by a ligase or other method, creating a pDNA sequence strand (510) specific for the protein molecule of unfolded protein (500).[000270] In some embodiments, the pDNA sequence strand can be used in a protein detection method using any one of the qPCR (singleplex or multiplex, probe or intercalation based) methods known to the skilled artisan. As depicted in Figs. 6A-6D, an unfolded protein, represented as amino acid sequence (401) in solution as illustrated in Fig. 6A with a mixture of a plurality of specific Conversome molecules added to the solution (Fig. 6B), the specific Conversomes bind to their respective cognate amino acid(s) (Fig. 6C). Concatenation of the trans-Decodon strands by a ligase (230) or other concatenation agent or method to create a pDNA sequence strand (660) is depicted in Fig. 6D. Figure 6E illustrates the addition of forward and reverse primers ((630) and (620)) and a probe (610) to be employed in qPCR following denaturation and release of the pDNA sequence strand (670) and hybridizing the primers and probe for the initiation of qPCR by 5’ nuclease (Fig.6F).[000271] Alternatively, the pDNA strand can have added Primers ((630 and (620)) for intercalation based qPCR (Fig. 6G) following denaturation and release of the pDNA sequence strand (670) and hybridizing the primers for the initiation of intercalation based qPCR (Fig. 6H).[000272] In another alternative, following concatenation of the Decodon strands, (Figs. 7A-7D), addition of a panel of sequencing primer pairs (Fig. 7E), targeting different pDNA strands are added following pDNA concatenation (660) for NGS targeting. The denaturation of the concatenated different pDNA strands allows PCR primer pairs to hybridize to the released, concatenated different pDNA strands for PCR amplification of different pDNA strands in targeted Next Generation Sequencing (NGS) processes (Fig.7F). Further details can be found in standard targeted-amplicon next-generation sequencing workflow descriptions available in the NGS methods literature.[000273] In some embodiments, the process following concatenation of the Decodon strands (660), (Figs. 8A-8D), addition and attachment of different DNA sequencing adapters (only (800) and (810) are illustrated, Fig. 8E), to every pDNA sequence strand (e.g., (885) and (880)) to convert the pDNA sequences into library molecules ((887) and (882), Fig. 8G) for analysis by NGS. Further details on short-insert performance are available in Illumina technical bulletins on library insert size and sequencing performance.[000274] In some embodiments, targeted protein molecule detection can be achieved using pre-linked amino acid recognition portions as illustrated in Figure 10. Using pseudo-Conversomes pre-linked Ligamers elements (1000) can be used for detection of specific amino acid sequences in a target protein. Single-stranded nucleic acids or other types of chemical linkages are attached to a first end of two or more Linker elements and pre-link each of a first end of each of two or more Linker elements whose opposite, second ends are each attached to at least one or more Ligamer element’s amino acid recognition portion(s), creating pre-linked Ligamer elements. Addition of the pre-linked Ligamer elements to the solution containing a target protein allow the pre-linked Ligamers’ amino acid recognition portions to bind to their comparably positioned reciprocal / cognate amino acids within the target protein. Detecting the protein sequence can then be done via the pre-linked Ligamers’ single-stranded nucleic acids or other types of chemical linkages which can also be connected to a Detection molecule (901) including, but not limited to, a fluorescent molecule or via an enriched immunoprecipitation assay via a linked bead (901).[000275] Figure 11 illustrates how a protein molecule’s sequence is detected without pre-linking specific Conversome molecules. As illustrated in Fig. 11 A, a mixture of a plurality of different specific Conversome molecules (1100, 1110, 1120, 1130, 1140, and 1150), each Conversome molecule with a specific single strand cis-Decodon strand, is added to a mixture of unfolded polypeptide sequences (401). The specific Conversomes can bind to each Conversome’s specific cognate amino acid via each different Conversome molecule’s amino acid specific Ligamer portion (Fig. 11B). A specific, labeled, complementary targeting oligonucleotide nucleic acid sequence strand ((1170), Fig. 11C) that targets / recognizes specific cis-Decodon nucleic acid sequences within the target protein’s amino acid sequence is added to the solution and can bind to a specific series of Conversomes’ single-stranded cis-Decodon strands along the unfolded polypeptide (401) sequence (Fig 11 D) within the target protein’s amino acid sequence. Detecting the target protein’s sequence can then be done via the complementary oligonucleotide nucleic acidstrand (1170) connected to at least one of a fluor, enzyme, enriched via immunoprecipitation, or captured if a magnetic bead ((901) FIG. 11D) is attached to the complementary oligonucleotide sequence.[000276] In another aspect disclosed is a process for detecting the presence or absence of at least one specific protein in a sample by secondary or tertiary structures of the protein in a natural state. The process begins with the addition to an intact protein in its natural state a mixture of a plurality of different, specific Conversome molecules (Fig. 12A). When proteins are folded in the native state there are some amino acids ((e.g. (202), (206), (205) and (204)) that are accessible as illustrated in Fig. 12B, and bound by their specific Conversome molecule. It is noted that amino acid (203) is an inaccessible amino acid and remains an unbound cognate amino acid for Conversome molecule (213). Figures 12C and 12D illustrate the concatenation of trans- Decodon strands which are in interlocking spatial proximity to other bound Conversomes. This creates a “pattern” based on the Conversomes that are close to each other. Monitoring the protein’s secondary and tertiary structures can result in changes in the “pattern” as changes in structure will change which Conversomes can concatenate to one another. As depicted in Figure 12E concatenation occurs between bound Conversomes’ trans-Decodon double-stranded nucleic acid sequences in interlocking spatial proximity to other bound Conversomes’ trans-Decodon double-stranded nucleic acid sequences (1200) following their concatenation. The concatenated pDNA sequence strand (1210) can be denatured to release the pDNA sequence strand from its complementary cis-Decodon strand to be used in and detected by qPCR and other methods known to the skilled artisan. Example 10 provides a prophetic example for determining the 3D structure of a protein.[000277] In another aspect, the disclosed process can be used in a method to detect protein:protein interactions and quaternary structure. As illustrated in Fig. 13A a solution of two proteins in a natural state (1300) and (1310) are interacting and a mixture of a plurality of different, specific Conversome molecules is added. When proteins are folded in the native state there are some amino acids ((e.g. (202), (206), (205) and (204)) that are accessible for binding by Conversome molecules. As illustrated in Fig. 13B, accessible amino acids exist within protein(s) in the natural state and each can be bound by their specific Conversome molecule. It is noted that amino acid (203) is an inaccessible amino acid and remains an unbound cognate amino acid for Conversome molecule (213). Figures 13C to 13D illustrate treatment of the Decodon strands with a concatenating agent and the concatenation of trans-Decodon strands from bound Conversome molecules ((212), (216), (215)) in interlocking spatial orientation to one another to form a concatenated polynucleotide strand specific oligonucleotide nucleic acid sequence (pDNA sequencestrand) representing the two protein molecules interacting with one another in their natural state. This creates a “pattern” based on the Conversomes that are close to each other. Monitoring the proteins’ structures and interactions can result in changes in the “pattern” as changes in structure will change which amino acids are accessible which in turn changes which Conversomes molecules can access and bind to their cognate amino acid and in their interlocking angle to other bound Conversome molecule’s Decodon strands to concatenate with one another. As depicted in Figure 13E concatenation occurs between bound Conversomes’ trans-Decodon double-stranded nucleic acid sequences in interlocking spatial orientation to other bound Conversomes’ trans-Decodon doublestranded nucleic acid sequences (1200). Following concatenation (Fig. 13F), the pDNA sequence strand (1210) (the released concatenated trans-Decodon strands (1200)) undergoes denaturation and detection in any of the methods including, but not limited to, NGS, qPCR and / or if a Detection molecule (901) is attached at the 5’ end of the pDNA sequence strand comprising a fluor or enzyme, or enriched via immunoprecipitation, a bead with different density, or captured if a magnetic bead (or other affinity reagent) is present (Detection molecule not shown, see Fig. 11D for illustration of an attached Detection molecule). Example 11 provides an illustrative example for determining / detecting protein: protein interactions.[000278] In another aspect the disclosed process can be used for detecting the presence of modified amino acid(s) in a protein sample(s). Figures 14A-14E illustrate an example of this process. The process comprises treating both a first control natural protein sample (1401) and a second suspect protein sample(s) (1404) suspected of having a modified amino acid under denaturing conditions such that the first control protein and second suspect protein sample(s) each forms into an unfolded control and unfolded suspect protein(s) polypeptide sequences, respectively (Fig. 14A). The amino acid modification can include, but is not limited to, at least one of a phosphorylation, acetylation, N-linked glycosylation, Amidation, hydroxylation, methylation, O-linked glycosylation, Ubiquitylation, Pyrrolidone carboxylic acid, and Sulfation as known to the skilled artisan. A mixture of a plurality of different, specific Conversome molecules is added to each protein sample (Fig. 14B). One of these Conversomes recognizes the natural amino acid (212), and a second different, specific Conversome with a different Decodon sequence recognizes the corresponding, modified amino acid (1414). Figure 14C shows the mixture of the plurality of Conversomes binding to their cognate amino acids to both the first unfolded control and second unfolded suspect protein polypeptide sequences. The bound Conversomes’ Decodon elements are treated with a concatenating agent such as a ligase or other method creating a pDNA sequencing strand, or a nucleotide polymer from an amino acid polymer. The concatenated pDNA sequence strands (1420) and (1430)(concatenated trans-Decodon strands) undergoes denaturation and detection in any of the methods including, but not limited to, NGS, qPCR and / or if a Detection molecule (901) is attached at the 5’ end of the pDNA sequence strand comprising a fluor or enzyme, or enriched via immunoprecipitation, a bead with different density, or captured if a magnetic bead (or other affinity reagent) (Fig. 14E), (Detection molecule not shown, see Fig. 11 D).[000279] Detection of the modification is illustrated in Fig. 14E. Examination by sequencing the pDNA sequence strands of the released, concatenated pDNA oligonucleotide nucleic acid sequence strands ((1420) and (1430)) and looking for the presence or absence of a modified amino acid nucleic acid identifier (G-T-G) in the sequence from the second unfolded, suspect protein (1430) is visible in Fig. 14E and shows comparing the sequencing products to see if the modified Decodon strand’s DNA oligonucleotide nucleic acid pDNA sequence strand is present; presence of the modified Decodon strand’s DNA nucleic acid (G-T-G) in the pDNA sequence strand within the concatenated DNA of the suspect unfolded second protein is affirmative for the presence of a modified amino acid in the suspect protein. Of note is that the two pDNA sequence strands are identical except for one Decodon strand’s sequence which represents the natural, unmodified amino acid (1420) whose Conversome molecule’s trans-Decodon sequence is found in the control protein, (A-T-A), and is present in the control pDNA sequence strand and the different specific Conversome molecule’s trans-Decodon sequence found with an amino acid recognition portion and specific Decodon strand sequence (G-T-G) specific for the modified amino acid (1430) is only found in the pDNA sequence strand of the suspect protein. Example 12 provides an illustrative example for detecting post-translational protein modifications at the level of the protein’s amino acids.[000280] Figures 15A and 15B illustrate different Decodon types. Although the drawings present three nucleic acid base pairs for both a single strand and a double strand amino acid specific Decodon strand, the drawings are illustrative only and should not be limiting; any number of nucleic acids described herein may be utilized. Orientation and directionality of Decodon strands can be directed by arrangement of nucleic acids at the ends of the single strand and double strand Decodons. A blunt ended single and double strand Decodon strand can be oriented in either the 5’ or 3’ end of the resulting pDNA sequence strand. The Decodon strand’s ends can have 1 to 35 or more bases overhanging at either the 5’ or 3’ ends (Fig. 15A).[000281] Decodon single- and double-stranded ends can also have, either alone or in addition to overhanging ends, ends with one or more of a OH, PO4, H, or blocked (Detection molecule(s) (901). As depicted in Fig. 15B, an H or a block (901) on one end (side of the Decodon) leaves the opposite end with an OH and PO4 available toconcatenate. The presence of OH and PO4 on single- and double-stranded Decodon strands ends allows for concatenation on both ends while the presence of H on one end of the single-stranded Decodon strand and both ends of the double-stranded Decodon strand and either OH or PO4 on the single strand Decodon strand and either OH and PO4 at the ends of the complementary strand indicates that the strand with OH and / or PO4 is the strand available to concatenate (Fig. 15B).[000282] Figure 15B demonstrates modifications to the Decodon strand’s ends which can limit the orientation of concatenation by either blocking (901) or not providing the active moiety on the other end of either the single or double-stranded Decodon strand.[000283] Figure 15C illustrates a Detection Molecule on one end of the Decodon strand, blocking the end from concatenation. The opposite ends of each strand can concatenate.[000284] Figure 15D illustrates the presence of Hydrogen (H) on both complementary strands at the same end of double-stranded Decodon strands, leaving the opposite ends of the complementary strands available to concatenate.[000285] Figure 15E illustrates all four ends of double-stranded Decodon strands available to concatenate as each end has an active moiety, either an OH or a PO4.[000286] Figure 15F illustrates the presence of Hydrogen (H) on both ends of one complementary strand of double-stranded Decodon strands being blocked from concatenating, leaving the other complementary strand available to concatenate.[000287] For DNA and RNA oligonucleotides the 5' end designates the position at the fifth carbon in the sugar-ring of the deoxyribose or ribose of the terminal nucleotide. The 3' end designates the position at the third carbon in the sugar-ring of the deoxyribose or ribose of the terminal nucleotide. T4 DNA Ligase uses a PO4 group at the 5' end and an OH at the 3' end in order for the enzyme to form a phosphodiester bond. Replacing either with a H would not provide the correct substrate for ligation.[000288] In some embodiments, the Conversome molecule can be constructed to detect two different corresponding, specific amino acids (adjacent or non-adjacent to each other) on the same polypeptide strand. The Conversome molecule’s Ligamer element can be modified to have two different, cognate amino acid recognition / binding portions (1602 and 1604) linked to one Decodon element having a double strand (or single strand), specific oligonucleotide nucleic acid sequence (1606 and 1608). Fig. 16A illustrates each of two Conversome molecules (1600 and 1601) whose Ligamer elements each have two amino acid recognition portions for binding to two cognate amino acids, either adjacent orin interlocking spatial orientation, on the same polypeptide strand. Example 11 provides an illustrative example for determining / detecting protein: protein interactions.[000289] In some embodiments, the OligoConversome molecules can be used in the data analysis of protein isoforms to quantify the protein isoforms in a normal versus a diseased state(s). The bar graph of Fig. 17 illustrates protein isoforms using OligoConversomes and qPCR at Initial Disease Diagnosis (Time point 1). Normal (disease-free) samples will predominantly have isoform 1, and there will be a 1:1 ratio of isoform 1 and isoform 2 in an early disease sample. Time point 2 will show Isoform 1 measurements are predominant in normal samples and Diseased samples will exhibit a significant increase in isoform 2 measurements relative to Isoform 1 measured levels, indicating disease progression. Following treatment (Timepoint 3), the treated disease samples exhibit an increase in isoform 1 vs. isoform 2 suggesting there will be treatment effectiveness seen as reducing isoform 2 measured levels. The sample can be obtained from a cell, tissue, organ or organism, from one or more organisms, organ, tissue or cell. The types of proteins in the sample can be a mixture selected from two or more of enzymes, structural, cell signaling, extracellular proteins, signal transduction, receptors, membrane proteins, transmembrane proteins, antibodies, ligand transport proteins, Lectins, fibrous proteins, receptors and hormones. Example 13 provides an illustrative example for using OligoConversomes and qPCR to distinguish protein isoform analysis, disease detection, and data analysis of protein quantity in normal vs. diseased samples.[000290] In some embodiments, Conversome molecules can be used to identify protein expression patterns in a patient population but can also provide predictive analytics of both immediate, interim, and long-term disease conditions, risks and projections.[000291] Figure 18 illustrates 50 patients’ Proteome analysis. Next Generation Sequencing of pDNA is prepared from each patient and data will be visualized as clusters of similar proteome profiles using Uniform Manifold Approximation and Projection (UMAP) or similar analysis tool. Example 14 provides an illustrative example for using Conversome molecules with NGS of pDNA to analyze proteome expression patterns, to distinguish protein isoform analysis, disease detection, and data analysis of protein quantity in normal vs. diseased samples.[000292] In some embodiments, a splint oligonucleotide nucleic acid sequence (splint oligo) can be used to concatenate single strand cis-Decodon strands to detect or identify a target protein molecule. Figure 19 illustrates the disclosed innovation using targeted Conversome molecules’ cis-Decodon strands nucleic acid sequences, not pre-linked, for detection of specific target protein(s) sequences. As depicted in Figure 19A Conversome molecules (1100, 1110, 1120, 1130, 1140, and 1150) with single strand cis-Decodonstrands in their Decodon elements are added to an unfolded target protein sample (401). The Conversomes bind to their cognate amino acids (Figure 19B). A splint oligonucleotide nucleic acid sequence (1902) is added to the solution of bound Conversomes with single strand cis-Decodons (Figure 19C) followed by the splint oligo binding to its cognate sequence, the single strand cis-Decodons (Figure 19D). Addition of a concatenating agent (230) concatenates the cis-Decodon strands that are bound by the splint oligo (Figure 19E to 19G) resulting in the splint oligonucleotide bound to the concatenated cis-Decodons (1904). The denaturation and release of the splint oligonucleotide bound to the concatenated cis-Decodons provides a pDNA sequence strand for use in qPCR or other methods known to the skilled artisan for protein detection using the pDNA sequence (1906). The pDNA sequence finds utility in a variety of methods as illustrated in the accompanying Drawings.[000293] In another aspect, disclosed are kits for determining the amino acid sequence of a Protein molecule. The kit can comprise: a.) a plurality of a mixture of specific Conversome molecules for each of 20 proteinogenic amino acids, exclusive of Selenocysteine and Pyrrolysine or b.) 20 vials of Conversome molecules, one vial for each of 20 specific proteinogenic amino acids, exclusive of Selenocysteine and Pyrrolysine; c.) a concatenating agent such as T4 DNA ligase, and d.) Instructions for use of Conversome molecules and the non-specific Conversome molecule. Optionally, the kit can further have e.) at least a vial each of specific Conversome molecules for each of Selenocysteine and Pyrrolysine amino acids; and / or f.) at least one vial of a plurality of a non-specific Conversome molecule.[000294] Additionally each of the Conversome molecules’ and the non-specific Conversome molecule’s Decodon element’s Decodon strands are either single strand specific and single strand universal cis-Decodon oligonucleotide nucleic acid sequence strands, respectively or double-stranded specific and double-stranded universal cis-Decodon oligonucleotide nucleic acid sequence strands, respectively. Also, either the single strand specific and single strand universal cis-Decodon oligonucleotide nucleic acid sequence strands, respectively or double-stranded specific and double-stranded universal cis-Decodon oligonucleotide nucleic acid sequence strands, respectively can have at least one blocked 5’ and / or 3’ end(s); wherein the at least one blocked 5’ and / or 3’ end(s) is selected from the group consisting of a Detection molecule on one end of the single, double or non-specific single or double cis-Decodon strand or on one end of one strand of the specific Conversomes’ or non-specific Conversome molecule’s double-stranded cis- or complementary trans-Decodon strands, a Hydrogen (H) on each end of the single, double or non-specific single or double cis-Decodon strand or on each end of one strand of thespecific Conversomes’ or non-specific Conversome molecule’s double-stranded cis- or complementary trans-Decodon strands, and an H at one end of both complementary ends of the specific Conversomes’ or non-specific Conversome molecule’s two double-stranded cis- and complementary trans-Decodon strands; wherein the end of the strand with the Detection molecule or H(s) are blocked from concatenation with adjacent or proximal specific Conversome molecules’ or non-specific Conversome molecule’s Decodon elements’ either single cis-Decodon strand or at least one strand of double strand cis- and complementary trans-Decodon strands oligonucleotide nucleic acid sequence(s).[000295] In another aspect, a second kit having extra reagents or an otherwise optional item can provide cost savings to the user. The kit will have: a.) the non-specific Conversome molecule further comprising either a Decodon element whose single strand Decodon strand’s oligonucleotide nucleic acid sequence is a cis-Decodon strand or a double-stranded Decodon element with cis- and complementary trans-Decodon strand’s oligonucleotide nucleic acid sequences; b.) T4DNA ligase; and c.) Instructions for use.[000296] In yet another aspect, a third kit for determining the amino acid sequence of a Protein molecule will have: a) a plurality of a mixture of at least two or more specific Conversome molecules for each of 20 proteinogenic amino acids, exclusive of Selenocysteine and Pyrrolysine; or b.) 20 vials of Conversome molecules, one vial for each of 20 specific proteinogenic amino acids, exclusive of Selenocysteine and Pyrrolysine; wherein at least two specific Conversome molecules are pre-linked by their respective Decodon element’s Decodon strand(s) oligonucleotide nucleic acid sequence(s) prior to binding to their respective cognate amino acid(s) forming OligoConversome molecules; c.) T4 DNA ligase; and d.) Instructions for use of the pre-linked specific OligoConversome molecules and non-specific Conversome molecules.[000297] Optionally, the kit can further have e.) at least a vial each of specific OligoConversome molecules for each of Selenocysteine and Pyrrolysine amino acids; and / or f.) at least one vial of a plurality of a non-specific Conversome molecule.[000298] Additionally each of the OligoConversome molecules’ and the nonspecific Conversome molecule’s Decodon element’s Decodon strands are either single strand specific and single strand universal cis-Decodon oligonucleotide nucleic acid sequence strands, respectively or double-stranded specific and double-stranded universal cis-Decodon oligonucleotide nucleic acid sequence strands, respectively. Also, either the single strand specific and single strand universal cis-Decodon oligonucleotide nucleic acid sequence strands, respectively or double-stranded specific and double-stranded universal cis-Decodon oligonucleotide nucleic acid sequence strands, respectively can have at least one blocked 5’ and / or 3’ end(s); wherein the at least one blocked 5’ and / or 3’ end(s) isselected from the group consisting of a Detection molecule on one end of the single, double or non-specific single or double cis-Decodon strand or on one end of one strand of the specific OligoConversomes’ or non-specific Conversome molecule’s double-stranded cis- or complementary trans-Decodon strands, a Hydrogen (H) on each end of the single, double or non-specific single or double cis-Decodon strand or on each end of one strand of the specific Conversomes’ or non-specific Conversome molecule’s double-stranded cis- or complementary trans-Decodon strands, and an H at one end of both complementary ends of the specific OligoConversomes' or non-specific Conversome molecule’s two doublestranded cis- and complementary trans-Decodon strands; wherein the end of the strand with the Detection molecule or H(s) are blocked from concatenation with adjacent or proximal specific OligoConversome molecules’ or non-specific Conversome molecule’s Decodon elements’ either single cis-Decodon strand or at least one strand of double strand cis- and complementary trans-Decodon strands oligonucleotide nucleic acid sequence(s).[000299] The current disclosure addresses the need in the art for easily converting all proteins within a cell, bodily fluid sample, tissue, biopsy, organ biopsy, proteome, environmental sample, bacterial sample, 3-D printed sample, irrespective of sequence and amount, into a format that could be detected and quantified. This can be through converting an entire proteome into DNA (or RNA) sequences for use in quantitation and identification of protein sequences from each protein’s corresponding DNA / RNA sequence. This can be accomplished through construction of amino acid specific adapter / recognition molecules to identify each of the amino acids, in the order they exist, within the proteome, protein, peptide or polypeptide sequence analyzed.[000300] The design of the Ligamer can be chosen such that it recognizes just one amino acid, or can recognize two, three, four, five, six, seven, eight, nine, ten, or more amino acids, either adjacent or in interlocking spatial orientation, at one time.[000301] Aptamers[000302] Aptamers provide one of the most straightforward approaches to generate a complete collection of the highly specific amino acid-binding moieties.[000303] Aptamer modifications[000304] Prerequisites for a successful application of RNA and DNA aptamers are represented by high affinity and selectivity to their target as well as by adequate stability against degradation (that can be caused by nucleases, metal ions, buffers with extreme pH, high temperature).[000305] Small molecules[000306] Several articles described efforts toward the development of the designed small molecules, capable of recognizing histidine or phosphorylated amino acid residues on peptide surfaces in a sequence-selective manner. These results demonstrate that cooperative metal-ligand interaction is powerful for tight and selective binding to the specific amino acid residues of proteins in aqueous medium. Presumably, some of these molecules can recognize and selectively bind to the individual amino acids as well.[000307] The palladium^ I)- ethylenediamine dinitrate complex.[000308] [Pd(ethylenediamine)(NO3)2] (Pd(en)) was used as a simple artificial receptor for the recognition of histidine residues presented on alpha-helical peptides (Hamachi et al., Chem Lett 2001, 16-17).[000309] The dipicolylamine Zn(ll) complex (Zn(Dpa)) was utilized as a binding module for histidine residues presented on the helical surface of the peptide (Mito-oka et al., Tetrahedron Lett 2001, 42, 7059-7062).[000310] It was discovered that the receptors Zn(Dpa)-1 ,8-Anth and Zn(Dpa)- 9,10-Anth possessing the two sets of zinc(ll)-Dpa (dipicolylamine), juxtaposed separately at the appropriate distance, can work as a binding motif toward phosphate species (Ojida et al., Biopolymers 2004, vol. 76, 177-184).[000311] Molecularly imprinted polymers[000312] A Molecularly Imprinted Polymer (MIP), or plastic antibody is a polymer that is formed in the presence of a molecule that is extracted afterwards, thus leaving complementary cavities behind. These polymers show a certain chemical affinity for the original molecule and can be used to fabricate sensors, catalysis or for separation methods (http: / / en.wikipedia.org / wiki / Molecular_imprinted_polymer).[000313] Host Guest Chemistry[000314] In supramolecular chemistry, host-guest chemistry describes complexes that are composed of two or more molecules or ions that are held together in unique structural relationships by forces other than those of full covalent bonds. Host-guest chemistry encompasses the idea of molecular recognition and interactions through noncovalent bonding. Noncovalent bonding maintains the three-dimensional structure of large molecules, such as proteins and is involved in many biological processes in which large molecules bind specifically but transiently to one another. There are four commonly mentioned types of non-covalent interactions: hydrogen bonds, ionic bonds, van der Waals forces, and hydrophobic interactions. (Freeman et al., Acta. Crystallogr. B40, 1984, 382-387.)[000315] LINKERS[000316] Examples are PEG of different lengths. The Linker element can be selected from the group including, but is not limited to, a linker consisting of Ethylene glycol, Polyethylene glycol (PEG), Glycerol, Aminopurine, Carbon spacer, Hexanediol, Dideoxyribose, a PC (Photo-Cleavable) Spacer, Melamine, Phenolic and Dialdehydes, Poly(N-(2-hydroxypropyl)methacrylamide, Alpha-D-Glucose, G1 PAMAM dendrimer, sulfonic acid group, glutathione, Poly-L-glutamic acid, and urethane.[000317] Characteristics and ways to utilize the disclosed Decodon strand and Decodon element include, but are not limited to, an end of the Conversome molecule having a specific sequence (reverse codon) for each amino acid but the oligonucleotide nucleic acid sequence can be a dimer, trimer, could be longer, a 26-mer, about 70 to 300 nucleic acids in length.[000318] Reverse codon could be attached to linker with click chemistry.[000319] If modified amino acids have different amino acid recognition portions, and a slightly different reverse codon, e.g., GCA to GTA could use a SNP assay for qPCR “genotyping”.[000320] Decodons could have overhangs in order to improve ligation efficiency.[000321] Concatenation of an amino acid sequence and a protein are more likely to happen in solution because the reverse codons are in interlocking spatial orientation.[000322] Ligation in solution is not an issue if doing TaqMan since amplicon sequence will be made randomly in solution at a lower rate.[000323] The cis-Decodon end or strand could also be made so that it is degraded by a chemical reaction.[000324] Sequencing would be discovery, and could find positions where proteins are modified.[000325] Connection Chemistries:[000326] A number of chemical bonding agents, binding methods and attachment / detection methods can be employed during the utilization of the Conversome Molecules for their creation, their attraction and binding to target amino acids, concatenation and ligation of pDNA sequence strands as well as in the creation of sequencing libraries and as tools for analyses of protein molecules. Provided below are afew types and structural arrangements that utilize connection chemistries including, but not limited to: and chemical agents or binding process.[000327] Concatenation[000328] Ligation[000329] Broadly defined, ligation refers to two nucleic acids joining together. Often in the field of molecular biology the reaction is catalyzed by an enzyme such as T4 DNA ligase. The reaction results in the formation of a phosphodiester bond between a 5’-phosphate group (-PO4) at one end of a strand of DNA and a 3’-hydroxyl group (-OH) at the 3’ end from a second DNA strand. Enzymes used in ligation include, but are not limited to: T4 DNA Ligase, RtcB Ligase, T3 DNA Ligase, T7 DNA ligase, E. coli DNA Ligase, SplintR Ligase, TaqDNA Ligase, 9°N DNA Ligase, T4 RNA Ligase 1, T4 RNA Ligase 2, Aminoacyl tRNA synthetase, Succinyl coenzyme A synthetase, Thiokinase, Ubiquitin Ligase, argininosuccinate synthetase, Gamma-glutamyl carboxylase, Polyketide synthase, DNA Ligase, Chelatases, Glutamate-cysteine ligase.[000330] Chemical Concatenation Processes[000331] There are a variety of chemical methods for joining nucleic acids including, but not limited to Click Chemistry, reductive amination, and phosphoramidite chemistry.METHODS[000332] Identification of new proteins[000333] The disclosed innovation has vast and varied applications and methods for elucidating the proteome of an individual, organism, organ, tissue and cell. New proteins can be proteins heretofore previously unidentified and / or unknown proteins. The fields of use are just as varied and include, but are not limited to the fields of:[000334] Drug discovery[000335] Development pathway analysis[000336] Pharmaceutical development[000337] Therapeutic development[000338] Diagnostics[000339] Genomic research[000340] Personalized medicine[000341] Forensics[000342] Disease and / or Infection identification / detection including a.) Disease diagnosis and b.) Disease staging.[000343] Animal medicine[000344] Prokaryotic Identification, and[000345] Pathogen detection[000346] Quantitation of a protein within a protein mixture.[000347] p53 protein levels are tightly regulated and vary depending on the cell's environment (e.g., high in cancer).[000348] Incorporated by reference is a manuscript forecasting the use of proteomic expression patterns and their use as prognosticators for disease and maladies years before clinical presentation. Using proteins to obtain “Differential expression [patterns] of many different proteins to get a “signature” of a sample (plasma proteins)” and use of proteomic data for clinically useful prediction of common and rare diseases by using predictor protein expression detection. (“Proteomic signatures improve risk prediction for common and rare diseases” Carrasco-Zanini, J., Pietzner, M., Davitte, J. et al. Nat Med 30, 2489-2498 (2024)).[000349] Figure 18 provides data analysis of the proteome for 50 patients using UMAP to cluster similar protein expression profiles. The analysis uses Next Generation Sequencing of pDNA molecules. Each sample will be measured in duplicate and combined before plotting. Each data point represents a quantitative measurement of protein expression profiles that will be obtained through sequencing. The data points will be clustered using UMAP to capture similarities between the patients based on their proteome profiles. Samples with similar protein expressions will be grouped closer together, enabling the identification of patterns or differences across the dataset. For instance, "Sample I Profile 1" and "Sample I Profile 2" will show and illustrate a higher degree of similarity in their protein profiles, clustering closely together, whereas "Sample I Profile 6" stands apart, indicating unique protein expressions that differentiate it from the clusters of other protein expressions. This distinction could be attributed to specific proteins uniquely expressed in "Sample I Profile 6."[000350] Differential expression of many different proteins to get a “signature” of a sample (plasma proteins)[000351] Included herein is the use of proteomic data for clinically useful prediction of common and rare diseases by using predictor protein expression detection. (“Proteomicsignatures improve risk prediction for common and rare diseases” Carrasco-Zanini, J., Pietzner, M., Davitte, J. et al. Nat Med 30, 2489-2498 (2024)).[000352] Detection of alternatively spliced proteins[000353] Multiple isoforms of the Fas receptor protein are produced by alternative splicing. With exon 6 form of the Fas receptor, which promotes apoptosis, or programmed cell death.[000354] Detection of protein localization (after cell fractionation)[000355] Loss of the nuclear localization signal (NLS) in the sex-determining region Y protein (SRY) has been shown to be associated with XY sex reversal in Swyer syndrome.[000356] Protein localization within a body[000357] CRP (C-reactive Protein) rises in the blood in response to inflammation and infection.[000358] Cardiac Troponins release to bloodstream when heart muscle is damaged.[000359] Detection of post translational protein modifications (protein cleavage)[000360] Proteolytic cleavage of proproteins into active forms (e.g., TGF-b activation after cleavage promoting growth and differentiation).[000361] Detection of post translational protein modifications (amino acid modifications)[000362] Phosphorylation (e.g., MAP kinases in response to growth signals).[000363] Epidermal growth factor receptor (EGFR) mutations in cancer lead to constitutive phosphorylation and activation.[000364] Detection of translational mistakes[000365] Misincorporation of amino acids[000366] Frameshift errors with cystic fibrosis and Duchenne multiple sclerosis (MS)[000367] Ribosomal pausing e.g., amyotrophic lateral sclerosis (ALS) caused by RNA misfolding, Huntington’s disease ribosomes move slowly allowing proteins to misfold [000368] Determine 3D structure of a protein[000369] Prions are proteins that have misfolded and can cause other proteins to misfold as well. The term "prion" comes from "proteinaceous infectious particle".[000370] Determination / detection of protein: protein interactions.[000371] During initiations of DNA replication multiple proteins are assembled together (the preinitiation complex, six ORC proteins (ORC1-6), Cdc6, Cdt1, and a heterohexamer of the six MCM proteins (MCM2-7))[000372] Small molecules[000373] A small molecule can cause protein degradation such as a Selective Estrogen Receptor Downregulator (SERD) like fulvestrant (Faslodex), which binds to the estrogen receptor and induces its degradation by the cell's natural protein degradation machinery; essentially marking it for destruction by triggering structural changes that expose degradation signals.EMBODIMENTS[000374] The following examples are provided for illustrative purposes only and not to limit the scope of the claims provided herein.[000375] Embodiment 1. A composition comprising: a residue-recognition moiety for reversibly or irreversibly binding to a residue of an amino acid or a residue of a polypeptide; optionally a linker moiety having a first end and a second end, the first end covalently or non-covalently coupled to the residue-recognition moiety; and a residuelabeling moiety comprising a nucleic-acid tag coupled to the second end of the linker moiety or directly to the residue-recognition moiety, the nucleic-acid tag comprising one or more nucleotides.[000376] Embodiment 2. The composition of Embodiment 1 , wherein the residue of the amino acid is a natural amino acid residue, selected from proteinogenic, non-proteinogenic, synthetic, or a post-translationally modified amino acid residues.[000377] Embodiment 3. The composition of Embodiment 1 , wherein the residue of the polypeptide is selected from proteinogenic, non-proteinogenic, synthetic, or a post-translationally modified polypeptide residues.[000378] Embodiment 4. The composition of Embodiment 1 , wherein the residuerecognition moiety comprises one or more of: an aptamer, oligonucleotide, polypeptide, peptide mimic, nanobody, antibody, antibody fragment, engineered scaffold protein, smallmolecule binder, metal-ligand complex, molecularly imprinted polymer, or combinations thereof.[000379] Embodiment 5. The composition of Embodiment 1 , wherein the residuerecognition moiety is not an antibody.[000380] Embodiment 6. The composition of Embodiment 1 , wherein the residuerecognition moiety reversibly or irreversibly binds to a residue of an amino acid or a residue of a polypeptide.[000381] Embodiment 7. The composition of Embodiment 1 , wherein the nucleic-acid tag is selected from the group consisting of: a ribonucleic acid (RNA) nucleotide, a deoxyribonucleic acid (DNA) nucleotide, a locked nucleic acid (LNA) nucleotide, a peptide nucleic acid (PNA) nucleotide, a threose nucleic acid (TNA) nucleotide, a glycol nucleic acid (GNA) nucleotide, a 1,5-anhydrohexitol nucleic acid (HNA) nucleotide, a cyclohexene nucleic acid (CeNA) nucleotide, a fluoroarabino nucleic acid (FANA) nucleotide, and any combination of the foregoing.[000382] Embodiment 8. The composition of Embodiment 1 , wherein the nucleic-acid tag has a length from 2 to 500 nucleotides, includes blunt and / or overhang termini, and comprises terminal chemistries selected from phosphate (PO4), hydroxyl (OH), hydrogen (H), ora blocking group.[000383] Embodiment 9. The composition of Embodiment 8, wherein the nucleic acid is single stranded or double stranded.[000384] Embodiment 10. The composition of Embodiment 1 , wherein the linker moiety comprises one or more of ethylene glycol, polyethylene glycol, glycerol, aminopurine, carbon spacers, hexanediol, dideoxyribose, photocleavable spacers, melamine, phenolics, dialdehydes, poly(N-(2-hydroxypropyl)methacrylamide), saccharides including alpha-D-glucose, dendrimers including PAMAM dendrimers, sulfonic acid groups, glutathione, poly-L-glutamine, poly-L-glutamic acid, urethane, or combinations thereof.[000385] Embodiment 11. The composition of Embodiment 1 , wherein the residuerecognition moiety is configured to bind to two or more residues that are adjacent to one another.[000386] Embodiment 12. The composition of any of Embodiments 1-11, wherein the nucleic-acid tag comprises a first tag strand and a complementary tag strand, and at least one strand includes an end modification limiting concatenation directionality.[000387] Embodiment 13. The composition of Embodiment 12, wherein the nucleic-acid tag is a hairpin nucleic-acid tag, a double helix nucleic-acid tag, or a triple helix nucleic-acid tag.[000388] Embodiment 14. The composition of any of Embodiments 1-13, wherein the residue-recognition moiety recognizes at least two amino acids that are not juxtaposed into one another.[000389] Embodiment 15. A composition comprising a plurality of residue-tagging monomers according to any of Embodiments 1-14, wherein the nucleic-acid tags are configured to be concatenated to one another in solution upon reaching an interlocking spatial alignment.[000390] Embodiment 16. A composition comprising a plurality of residue-tagging monomers according to any of Embodiments 1-15, wherein the nucleic-acid tag in one residue-labeling moiety is a first primer and the nucleic-acid tag in a second residuelabeling moiety is a second primer, whereby the first primer and the second primer support extension of a nucleic-acid sequence when two or more of the plurality of residue-tagging monomers in solution reach an interlocking spatial alignment.[000391] Embodiment 17. A composition comprising: a plurality of concatenated monomers, each monomer comprising: a residue-recognition moiety configured to recognize and bind to a residue of an amino acid or a residue of a polypeptide; optionally a linker moiety comprising a first end and a second end, wherein the first end is bonded to the residue-recognition moiety; and a residue-labeling moiety comprising a nucleic-acid tag comprising at least one nucleotide, wherein the residue-labeling moiety is bonded to the second end of the linker moiety or directly to the residue-recognition moiety; and whereby the plurality of concatenated monomers are concatenated at the residue-labeling moiety.[000392] Embodiment 18. The composition of Embodiment 17, wherein at least two nucleic-acid tags are pre-linked to each other prior to being added into the composition.[000393] Embodiment 19. The composition of Embodiment 17 or Embodiment 18, further comprising a non-specific residue-tagging monomer whose residue-recognition moiety binds indiscriminately to accessible residues and whose nucleic-acid tag is concatenation-compatible to fill unbound sequence positions.[000394] Embodiment 20. The composition of Embodiment 17 or Embodiment 18, further comprising a sub-set of residue-recognition moiety(ies) configured to recognize and bind to a sub-set of pre-determined residue(s) of an amino acid or a sub-set of predetermined residue(s) of a polypeptide(s).[000395] Embodiment 21. The composition of any of Embodiments 17-20, wherein concatenation is effected enzymatically or chemically, or with a combination thereof.[000396] Embodiment 22. The composition of any of Embodiments 17-21 , wherein concatenation is effected via a splint DNA that hybridizes to the plurality of concatenated monomers and extends its sequence via amplification.[000397] Embodiment 23. The composition of any of Embodiments 17-22, wherein the nucleic-acid tag in one residue-labeling moiety is a first primer and the nucleic-acid tag in a second residue-labeling moiety is a second primer, whereby the first primer and the second primer support extension of a nucleic-acid sequence when two or more of the plurality of residue-tagging monomers in solution reach an interlocking spatial alignment.[000398] Embodiment 24. A method of generating a protein-derived nucleic-acid readout from a peptide, polypeptide, or protein, the method comprising: providing a plurality of residue-tagging monomers according to any of Embodiments 1-23; contacting the peptide, polypeptide, or protein under conditions that render at least a portion of residues accessible; allowing the residue-recognition moieties to bind to their respective residues; concatenating at least a portion of the nucleic-acid tags of bound monomers to form a concatenated nucleic-acid sequence via interlocking spatial alignment of two or more residue-recognition moieties; and detecting the concatenated nucleic-acid sequence.[000399] Embodiment 25. The method of Embodiment 24, wherein rendering residues accessible comprises one or more of denaturation, fragmentation, backbone locking, helix stabilization, detergent treatment, or combinations thereof.[000400] Embodiment 26. The method of Embodiment 24 or Embodiment 25, wherein concatenation is mediated by an enzymatic ligase, a splint oligonucleotide, a chemical coupling reaction, or combinations thereof.[000401] Embodiment 27. The method of any of Embodiments 24-26, further comprising releasing the concatenated nucleic-acid sequence from the monomers by denaturation, linker cleavage, nuclease digestion of a complementary strand, heat, ionic, or chemical treatment.[000402] Embodiment 28. The method of any of Embodiments 24-27, further comprising detecting, identifying, or quantifying a protein, protein isoform, protein modification, secondary or tertiary structure, or protein-protein interaction using qPCR, digital PCR, next-generation sequencing, nanopore sequencing, Sanger sequencing, probe-based assays, or combinations thereof.[000403] Embodiment 29. The method of any of Embodiments 24-28, wherein the plurality comprises pre-linked residue-tagging monomers designed to target a predefined residue pattern.[000404] Embodiment 30. The method of any of Embodiments 24-29, further comprising adding a non-specific residue-tagging monomer to bind unoccupied residues before concatenation.[000405] Embodiment 31. A method of characterizing a protein's structural state comprising performing the method of any of Embodiments 24-30 under non-denaturing conditions and deriving an interlocking planar orientation-dependent concatenated nucleic-acid readout indicative of secondary, tertiary, or quaternary structure.[000406] Embodiment 32. A method of detecting a post-translational modification comprising performing the method of any of Embodiments 24-31 using residue-tagging monomers specific for a modified residue and its corresponding unmodified residue and distinguishing the presence of the modification by sequence differences in the concatenated nucleic-acid readout.[000407] Embodiment 33. The method of any of Embodiments 24-32, wherein, after allowing a mixture of a plurality of residue-recognition moieties to bind to their respective cognate residue of the amino acid or a residue of the polypeptide, an oligonucleotide that hybridizes to a residue-labeling moiety sequence associated with at least one bound residue-recognition moiety is added, and the bound residue of the amino acid or the residue of the polypeptide is detected by fluorescence readout or enriched by immunoprecipitation of the complex.[000408] Embodiment 34. The method of Embodiment 33, wherein the oligonucleotide is a splint oligonucleotide that hybridizes to a trans-residue-labeling moiety strand and comprises a capture or reporter moiety selected from biotin, digoxigenin, and a fluorophore.[000409] Embodiment 35. The method of Embodiment 34, wherein enrichment is performed by contacting the reaction mixture with a solid support which binds to a splint oligonucleotide or a trans-residue-labeling moiety strand hybridized thereto, followed by washing and elution of peptide-bound complexes.[000410] Embodiment 36. The method of Embodiment 35, wherein the solid support is streptavidin-coated magnetic beads to capture a biotinylated splint oligonucleotide or a biotinylated trans-residue-labeling moiety strand.[000411] Embodiment 37. The method of any of Embodiments 24-36, further comprising concatenating the residue-labeling moiety elements to generate a protein identifier DNA (pDNA) sequence corresponding to the sequence of amino acids contacted by the residue-recognition moieties and quantifying the pDNA by quantitative PCR.[000412] Embodiment 38. The method of Embodiment 37, further comprising sequencing the pDNA by nanopore or Illumina next-generation sequencing to determine the order of residue-labeling moiety sequence elements and thereby resolve the polypeptide sequence recognized by the residue-recognition moieties.[000413] Embodiment 39. The method of any of Embodiments 24-38, wherein the nucleic-acid tag in the residue-labeling moiety is a first primer and the nucleic-acid tag in a second residue-labeling moiety is a template oligonucleotide, and whereby the first primer and the second primer support extension of a nucleic-acid sequence when two or more of the plurality of residue-tagging monomers in solution reach an interlocking spatial alignment.[000414] Embodiment 40. The composition of any of the preceding composition embodiments, wherein the nucleic-acid tag length is 3-12 nucleotides and includes a 3' one-base overhang.[000415] Embodiment 41. The method of any of the preceding method embodiments, wherein concatenation uses SplintR ligase with a complementary splint oligonucleotide hybridizing to two adjacent tag strands.[000416] Embodiment 42. A kit comprising: a plurality of residue-tagging monomers according to any of Embodiments 1-23 targeting at least a subset of amino acid residues; at least one concatenation agent selected from an enzymatic ligase or a chemical coupling reagent; and instructions for use.[000417] Embodiment 43. The kit of Embodiment 42, further comprising one or more of: a non-specific residue-tagging monomer; a set of pre-linked residue-tagging monomers; a splint oligonucleotide; sequencing adapters; and PCR primer sets.[000418] Embodiment 44. The kit of Embodiment 42 or Embodiment 43, wherein the residue-tagging monomers are provided as single-stranded or double-stranded nucleic-acid tags with defined end chemistries to control concatenation orientation.[000419] Embodiment 45. The kit of any of the preceding kit embodiments, wherein the linker is photocleavable and configured to release the concatenated readout on exposure to light.[000420] Embodiment 46. The kit of any of the preceding kit embodiments, wherein the chemical coupling reagent is a nucleic acid extending enzyme, optionally wherein the nucleic acid extending enzyme is a DNA polymerase or an RNA polymerase.[000421] Embodiment 47. A specific Conversome molecule comprising: a Decodon element at a first end comprising a specific Decodon strand that is either a first singlestranded cis-Decodon oligonucleotide nucleic acid sequence or a double-stranded Decodon comprising a second single-stranded cis-Decodon oligonucleotide nucleic acid sequence and a complementary trans-Decodon oligonucleotide nucleic acid sequence, wherein each Decodon strand comprises 2 to 300 nucleic acids in length of a unique,specific, single- or double-stranded oligonucleotide nucleic acid sequence(s) selected from at least one nucleic acid type or a mixture of nucleic acid types, the group consisting of DNA, RNA, LNA, PNA, TNA, GNA, HNA, CeNA, and FANA; a Ligamer element at a second end, opposite the first end, comprising at least one amino acid recognition portion for binding to at least a first, cognate, specific amino acid within a protein molecule; and a Linker element between and connecting the first end Decodon element and the second end Ligamer element; wherein the specific Conversome molecule recognizes and binds to its at least first cognate amino acid within the protein molecule.[000422] Embodiment 48. The specific Conversome molecule of Embodiment 47, wherein the protein molecule is selected from a peptide, a polypeptide, a protein, and a proteome.[000423] Embodiment 49. The specific Conversome molecule of Embodiment 47, wherein the protein molecule's amino acid is selected from one or more of a proteinogenic, non-proteinogenic, modified, and synthetic amino acid.[000424] Embodiment 50. The specific Conversome molecule of Embodiment 47, wherein the Ligamer element further comprises at least a second specific amino acid recognition portion for binding to at least a second, cognate, specific amino acid within the protein molecule.[000425] Embodiment 51. The specific Conversome molecule of Embodiment 50, wherein the Ligamer element's first and second specific amino acid recognition portions bind to adjacent first and second specific amino acids within the protein molecule.[000426] Embodiment 52. The specific Conversome molecule of Embodiment 47, wherein the double-stranded Decodon comprises ends selected from blunt ends; 1-, 2-, or 3-base 5' overhangs; and 1-, 2-, or 3-base 3' overhangs.[000427] Embodiment 53. The specific Conversome molecule of Embodiment 47, wherein the Decodon element's oligonucleotide nucleic acid sequence further comprises at least one strand with a blocked end, or wherein a hydrogen is attached to the third carbon atom of the deoxyribose or ribose sugar on one or each end of either or both strands, with no hydroxyl group at either end of either strand or at either end of one strand, wherein strand(s) with a blocked end or without a hydroxyl group are precluded from concatenation with adjacent or proximal Conversome Decodon element oligonucleotide sequence(s).[000428] Embodiment 54. The specific Conversome molecule of Embodiment 47, wherein the Decodon element's oligonucleotide nucleic acid sequence further comprises at least one strand with a blocked end, or wherein a hydrogen is attached to the fifth carbon atom of the deoxyribose or ribose sugar on one or each end of either or both strands, withno phosphate at either end of either strand or at either end of one strand, wherein strand(s) with a blocked end or without a phosphate are precluded from concatenation with adjacent or proximal Conversome Decodon element oligonucleotide sequence(s).[000429] Embodiment 55. The specific Conversome molecule of Embodiment 47, wherein the Decodon element's first single-stranded cis-Decodon strand is connected to the Linker element.[000430] Embodiment 56. The specific Conversome molecule of Embodiment 47, wherein the Linker element is selected from ethylene glycol, polyethylene glycol, glycerol, aminopurine, carbon spacer, hexanediol, dideoxyribose, a photocleavable spacer, melamine, phenolics and dialdehydes, poly(N-(2-hydroxypropyl)methacrylamide), alpha-D-glucose, G1 PAMAM dendrimer, sulfonic acid group, glutathione, poly-L-glutamic acid, and urethane.[000431] Embodiment 57. The specific Conversome molecule of Embodiment 47, wherein the protein molecule is denatured.[000432] Embodiment 58. The specific Conversome molecule of Embodiment 47, wherein the protein molecule's polypeptide backbone has undergone locking by a locked alpha-helix.[000433] Embodiment 59. The specific Conversome molecule of Embodiment 47, wherein the protein molecule comprises a mixture of proteins.[000434] Embodiment 60. The specific Conversome molecule of Embodiment 47, wherein the protein molecule comprises a mixture of two or more proteins to be identified and / or detected.[000435] Embodiment 61. The specific Conversome molecule of Embodiment 47, wherein the at least first cognate amino acid within the protein molecule bound by the Ligamer's at least one amino acid recognition portion is any one of twenty-two proteinogenic amino acids.[000436] Embodiment 62. The specific Conversome molecule of Embodiment 47, wherein the at least first cognate amino acid within the protein molecule is a non-proteinogenic amino acid, a modified amino acid, or a synthetic amino acid.[000437] Embodiment 63. The specific Conversome molecule of Embodiment 47, wherein the at least first cognate amino acid within the protein molecule is a modified amino acid.[000438] Embodiment 64. The specific Conversome molecule of Embodiment 47, wherein the Decodon strand is the first single-stranded cis-Decodon oligonucleotide sequence.[000439] Embodiment 65. The specific Conversome molecule of Embodiment 47, wherein the Decodon strand is the double-stranded Decodon comprising the second cis-Decodon strand and the complementary trans-Decodon strand oligonucleotide sequences.[000440] Embodiment 66. The specific Conversome molecule of Embodiment 64, wherein the first single-stranded cis-Decodon sequence is concatenated to a second Conversome molecule's Decodon element single-stranded cis-Decodon sequence, wherein the second Conversome's cis-Decodon is adjacent or in an interlocking spatial alignment to the first Conversome's cis-Decodon.[000441] Embodiment 67. The specific Conversome molecule of Embodiment 65, wherein the double-stranded Decodon strand's second single-stranded cis-Decodon strand and / or complementary trans-Decodon strand oligonucleotide sequences are concatenated to a second Conversome molecule's double-stranded Decodon strand's cis-Decodon and / or complementary trans-Decodon oligonucleotide sequences, wherein the second Conversome's double-stranded Decodon is adjacent or in an interlocking spatial alignment to the first Conversome's double-stranded Decodon.[000442] Embodiment 68. The specific Conversome molecule of Embodiment 67, wherein concatenation is a chemical concatenation selected from pi conjugation, sigma conjugation, and hyperconjugation.[000443] Embodiment 69. The specific Conversome molecule of Embodiment 68, wherein concatenation is a chemical concatenation selected from pi conjugation, sigma conjugation, and hyperconjugation.[000444] Embodiment 70. The specific Conversome molecule of Embodiment 47, wherein either the first single-stranded cis-Decodon or the double-stranded Decodon undergoes chemical concatenation by using a chemical concatenation agent or a chemical process.[000445] Embodiment 71. The specific Conversome molecule of Embodiment 70, wherein the chemical concatenation agent is an enzyme selected from T4 DNA Ligase, RtcB Ligase, T3 DNA Ligase, T7 DNA Ligase, E. coli DNA Ligase, SplintR Ligase, Taq DNA Ligase, 9°N DNA Ligase, T4 RNA Ligase 1, T4 RNA Ligase 2, aminoacyl tRNA synthetase, succinyl coenzyme A synthetase, thiokinase, ubiquitin ligase, argininosuccinate synthetase, gamma-glutamyl carboxylase, polyketide synthase, DNAligase, and chelatases; and the chemical process is selected from click chemistry, reductive amination, and phosphoramidite chemistry.[000446] Embodiment 72. The specific Conversome molecule of Embodiment 47, wherein an OligoDecodon element is formed when at least two or more different and / or identical specific Conversome Decodon elements are pre-linked to one another prior to incorporation into a mixture of a plurality of different specific Conversome molecules in a solution of at least one protein to be detected and / or identified.[000447] Embodiment 73. The specific Conversome molecule of Embodiment 72, wherein the at least two or more different and / or identical specific Conversome molecules pre-linked by respective OligoDecodon elements are termed OligoConversome molecules, which can be bi-, tri-, quad-, penta-, hexa-, deca-, or higher multi-OligoConversome molecules.[000448] Embodiment 74. The specific Conversome molecule of Embodiment 73, wherein the two or more OligoDecodon elements are linked through at least one of the trans-Decodon strand, the cis-Decodon strand, or both the cis- and trans-Decodon strands.[000449] Embodiment 75. The specific Conversome molecule of Embodiment 47, wherein binding of the Ligamer element's first amino acid recognition portion to its first cognate amino acid on a protein specifically identifies and / or defines the first cognate amino acid by either the first single-stranded cis-Decodon's or the double-stranded Decodon's oligonucleotide nucleic acid sequence strand.[000450] Embodiment 76. The specific Conversome molecule of Embodiment 47, wherein the amino acid modification is selected from phosphorylation, acetylation, N-linked glycosylation, amidation, hydroxylation, methylation, O-linked glycosylation, ubiquitylation, pyrrolidone carboxylic acid, and sulfation.[000451] Embodiment 77. Two or more specific OligoConversome molecules prelinked together, wherein each OligoConversome molecule comprises: two or more specific Conversome molecules each comprising a Decodon element at a first end comprising a specific Decodon strand comprising either a first single-stranded cis-Decodon oligonucleotide sequence or a double-stranded Decodon comprising a second cis-Decodon strand and a complementary trans-Decodon strand oligonucleotide sequence, wherein each Decodon strand is from 2 to 300 oligonucleotide nucleic acids in length of a unique, specific oligonucleotide sequence(s) selected from DNA, RNA, LNA, PNA, TNA, GNA, HNA, CeNA, and FANA; a Ligamer element at a second end comprising at least a first amino acid recognition portion for binding to at least a first cognate amino acid within a protein; and a Linker element between and connecting each Decodon and Ligamerelement for each Conversome molecule; wherein the two or more Conversome molecules are pre-linked by concatenating the first single-stranded cis-Decodon sequence from each of the two or more specific Conversome molecules, or by concatenating each of the second cis-Decodon and the complementary trans-Decodon oligonucleotide sequences within the two or more specific Conversome molecules' double-stranded Decodon elements; wherein a pre-linked, specific OligoConversome molecule recognizes and binds to each of the two or more specific Conversome molecules' at least first cognate amino acid within the protein.[000452] Embodiment 78. The two or more specific OligoConversome molecules prelinked of Embodiment 77, further comprising a detection molecule at the 5' end of the prelinked trans-OligoDecodon strand but not at the complementary pre-linked cis-OligoDecodon strand.[000453] Embodiment 79. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein detection is via fluorescence or enrichment via immunoprecipitation.[000454] Embodiment 80. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the protein molecule is selected from a peptide, a polypeptide, a protein, and a proteome.[000455] Embodiment 81. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the protein molecule's amino acid is selected from a proteinogenic, non-proteinogenic, modified, and synthetic amino acid.[000456] Embodiment 82. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the Ligamer element further comprises a second specific amino acid recognition portion for binding to a second specific amino acid within the protein.[000457] Embodiment 83. The two or more specific OligoConversome molecules prelinked of Embodiment 82, wherein the Ligamer element's first and second amino acid recognition portions bind to adjacent first and second specific amino acids within the protein.[000458] Embodiment 84. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the double-stranded Decodon comprises ends selected from blunt ends; 1-, 2-, or 3-base 5' overhangs; and 1-, 2-, or 3-base 3' overhangs.[000459] Embodiment 85. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the OligoDecodon element's double-strandedoligonucleotide sequence further comprises at least one strand with a blocked end, wherein a hydrogen is attached to the third carbon atom of the deoxyribose sugar on one or each end of both cis- and trans-OligoDecodon strands, with no hydroxyl group attached to either end of either strand or at either end of one strand, wherein the strand(s) with a blocked end or without a hydroxyl group are precluded from concatenation with adjacent or proximal OligoConversome OligoDecodon element sequences.[000460] Embodiment 86. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the OligoDecodon element's cis-OligoDecodon strand is connected to the Linker element; and wherein the Linker element is selected from ethylene glycol, polyethylene glycol, glycerol, aminopurine, carbon spacer, hexanediol,di deoxyribose, a photocleavable spacer, melamine, phenolics and dialdehydes, poly(N-(2-hydroxypropyl)methacrylamide), alpha-D-glucose, G1 PAMAM dendrimer, sulfonic acid group, glutathione, poly-L-glutamic acid, and urethane.[000461] Embodiment 87. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the protein molecule is denatured.[000462] Embodiment 88. The two or more specific OligoConversome molecules prelinked of Embodiment 87, wherein the denatured protein's polypeptide backbone has undergone locking by a locked alpha-helix.[000463] Embodiment 89. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the protein molecule comprises a mixture of proteins.[000464] Embodiment 90. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the first cognate amino acid within the protein bound by the Ligamer's first amino acid recognition portion is any one of twenty-two proteinogenic amino acids.[000465] Embodiment 91. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the first cognate amino acid within the protein bound by the Ligamer's first amino acid recognition portion is one of a non-proteinogenic amino acid, a modified amino acid, or a synthetic amino acid.[000466] Embodiment 92. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the specific cognate amino acid within the protein is a modified amino acid.[000467] Embodiment 93. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the first double-stranded OligoDecodon to be pre-linkedis the first double-stranded Decodon comprising the first cis-Decodon and its complementary trans-Decodon oligonucleotide sequences.[000468] Embodiment 94. The two or more specific OligoConversome molecules prelinked of Embodiment 93, wherein the first double-stranded OligoDecodon strands are prelinked by concatenation to the second double-stranded OligoDecodon strands by only each of the first and second trans-OligoDecodon strands within the first and second OligoDecodon elements, respectively.[000469] Embodiment 95. The two or more specific OligoConversome molecules prelinked of Embodiment 93, wherein the first double-stranded OligoDecodon strands are prelinked by concatenation to the second double-stranded OligoDecodon strands by both the first and second cis-OligoDecodon strands and both the first and second trans-OligoDecodon strands, respectively, wherein following concatenation, the first and second OligoDecodon elements are termed a first and a second OligoConversome molecule, respectively.[000470] Embodiment 96. The two or more specific OligoConversome molecules prelinked of Embodiments 94 and 95, wherein the first OligoConversome element is adjacent or in an interlocking spatial alignment to the first double-stranded OligoDecodon element.[000471] Embodiment 97. The two or more specific OligoConversome molecules prelinked of Embodiments 94 and 95, wherein the chemical concatenation is selected from pi conjugation, sigma conjugation, and hyperconjugation.[000472] Embodiment 98. The two or more specific OligoConversome molecules prelinked of Embodiments 94 and 95, wherein the double-stranded Decodon strands undergo chemical concatenation by using a chemical concatenation agent or a chemical process.[000473] Embodiment 99. The two or more specific OligoConversome molecules prelinked of Embodiment 98, wherein the chemical concatenation agent is an enzyme selected from T4 DNA Ligase, RtcB Ligase, T3 DNA Ligase, T7 DNA ligase, E. coli DNA Ligase, SplintR Ligase, Taq DNA Ligase, 9°N DNA Ligase, T4 RNA Ligase 1, T4 RNA Ligase 2, aminoacyl tRNA synthetase, succinyl coenzyme A synthetase, thiokinase, ubiquitin ligase, argininosuccinate synthetase, gamma-glutamyl carboxylase, polyketide synthase, DNA Ligase, and chelatases; and the chemical process is selected from click chemistry, reductive amination, and phosphoramidite chemistry.[000474] Embodiment 100. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the pre-linked OligoDecodon elements are termed OligoConversome molecules, which can be bi-, tri-, quad-, penta-, hexa-, deca-, or higher multi-OligoConversome molecules.[000475] Embodiment 101. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein the two or more OligoDecodon elements are linked through at least one of the first single-stranded trans-Decodon strands, at least one of the first single-stranded cis-Decodon strands, or both the double-stranded first cis- and first trans-Decodon strands.[000476] Embodiment 102. The two or more specific OligoConversome molecules prelinked of Embodiment 77, wherein binding of the Ligamer element's first amino acid recognition portion to its first cognate amino acid on a protein specifically identifies and / or defines the first cognate amino acid by either the first single-stranded cis-Decodon or the double-stranded first cis- and first trans-Decodon oligonucleotide sequence strands.[000477] Embodiment 103. The two or more specific OligoConversome molecules prelinked of Embodiment 92, wherein the amino acid modification is selected from phosphorylation, acetylation, N-linked glycosylation, amidation, hydroxylation, methylation, O-linked glycosylation, ubiquitylation, pyrrolidone carboxylic acid, and sulfation.[000478] Embodiment 104. The two or more specific OligoConversome molecules prelinked of Embodiment 82, wherein the OligoDecodon element's double-stranded oligonucleotide sequence further comprises at least one strand with a blocked end, wherein a hydrogen is attached to the fifth carbon atom of the deoxyribose sugar on one or each end of both cis- and trans-OligoDecodon strands, with no hydroxyl group attached to either end of either strand or at either end of one strand, wherein the strand(s) with a blocked end or without a hydroxyl group are precluded from concatenation with adjacent or proximal OligoConversome OligoDecodon element sequences.[000479] Embodiment 105. A process for detecting the presence or absence of at least one specific protein in a sample containing a mixture of proteins or distinguishing between two or more different proteins in the sample using the specific Conversome molecules of Embodiment 47, wherein the process comprises: treating the sample under denaturing conditions such that the mixture of proteins form unfolded polypeptide sequences; adding to the unfolded polypeptide sequences a mixture of a plurality of amino acid-specific Conversome molecules, wherein each Conversome Decodon element is either a singlestranded cis-Decodon or a double-stranded cis- and trans-Decodon, and each Ligamer binds its cognate amino acid within the unfolded polypeptide sequences; treating the bound Conversome Decodon elements with a concatenating agent, wherein the Decodon strands are concatenated to form a strand-specific oligonucleotide nucleic acid sequence(s) termed a concatenated pDNA or pRNA sequence strand(s), each representing a detectable unfolded polypeptide sequence(s); releasing and denaturing the concatenated pDNA or pRNA sequence strand(s) to make them available for detection;using the concatenated pDNA or pRNA sequence strand(s) to detect and / or identify the protein sequence(s) in the sample; and distinguishing between two or more different proteins in the sample or detecting and / or identifying at least one specific protein in the sample.[000480] Embodiment 106. The process of Embodiment 105, wherein the oligonucleotide nucleic acid sequence(s) is selected from DNA, RNA, LNA, PNA, TNA, GNA, HNA, CeNA, and FANA.[000481] Embodiment 107. The process of Embodiment 105, wherein the concatenated first pDNA oligonucleotide sequence is released from the Linker element by linking RNA to the Linker element followed by degradation of the RNA with at least one of temperature, divalent cations, RNase, or nuclease.[000482] Embodiment 108. The process of Embodiment 106, wherein the released, concatenated first pDNA sequence strand is specific for one unfolded polypeptide sequence corresponding to one protein that can be detected using the pDNA sequence strand.[000483] Embodiment 109. The process of Embodiment 105, wherein each Conversome Ligamer element is specific for only one amino acid selected from a standard proteinogenic amino acid, a modified amino acid, a non-proteinogenic amino acid, and a synthetic amino acid.[000484] Embodiment 110. The process of Embodiment 105, wherein the Linker is selected from ethylene glycol, polyethylene glycol, glycerol, aminopurine, carbon spacer, hexanediol, dideoxyribose, a photocleavable spacer, melamine, phenolics and dialdehydes, poly(N-(2-hydroxypropyl)methacrylamide), alpha-D-glucose, G1 PAMAM dendrimer, sulfonic acid group, glutathione, poly-L-glutamic acid, and urethane.[000485] Embodiment 111. The process of Embodiment 108, wherein protein detection is by qPCR, next-generation sequencing, TaqMan assay, and qRT-PCR.[000486] Embodiment 112. The process of Embodiment 105, further comprising, after adding the mixture of specific Conversome molecules and before concatenation, adding a mixture of identical, non-specific Conversome molecules having identical first ends comprising a non-specific Decodon within a non-specific Decodon element connected by a Linker to identical second ends comprising a non-specific Ligamer element; wherein each identical non-specific Ligamer binds to unbound amino acid(s) on the unfolded polypeptide sequence, followed by washing away unbound non-specific Conversome molecules.[000487] Embodiment 113. The process of Embodiment 112, wherein adjacent first ends, trans-Decodon strands, of consecutively bound Conversome molecules on the unfolded polypeptide sequence are concatenated together.[000488] Embodiment 114. The process of Embodiment 105, wherein prior to releasing the concatenated strand(s), primers and probes for 5' nuclease qPCR are added to the Conversome molecules bound and concatenated on the unfolded polypeptide sequence.[000489] Embodiment 115. The process of Embodiment 114, wherein following concatenation on the unfolded polypeptide sequence, the bound and concatenated Conversome molecules are further bound by qPCR primers for intercalation-based qPCR.[000490] Embodiment 116. The process of Embodiment 105, further comprising after release adding a panel of sequencing primer pairs targeting different pDNA strands following concatenation, wherein the concatenated strands allow primer pairs to hybridize to the released strand(s) for next-generation sequencing targeting by PCR amplification of different pDNA strands, wherein the pDNA strand(s) detect and / or identify at least one specific protein in the sample or distinguish between two or more different proteins.[000491] Embodiment 117. The process of Embodiment 105, wherein following concatenation adapters are attached to the ends of at least one strand of the concatenated Decodon pDNA strand(s) and the concatenated pDNAs are released and amplified for library preparation for next-generation sequencing.[000492] Embodiment 118. A process for detecting secondary or tertiary structures of a protein in a natural state comprising: adding to the sample a mixture of a plurality of different specific Conversome molecules of Embodiment 47, wherein each Decodon element is either single-stranded or double-stranded; binding the specific Conversome molecules to their accessible cognate amino acids; treating the bound Decodon elements with a concatenating agent such that at least one nucleic acid strand of each Decodon is concatenated with other bound Decodon strands to form a strand-specific pDNA sequence representing the protein in its natural state; treating to separate each concatenated pDNA strand from the bound Conversome molecules; detecting the protein based on the concatenated sequence to identify secondary or tertiary structures; and detecting the concatenated pDNA sequences by qPCR or next-generation sequencing.[000493] Embodiment 119. A process for detecting protein-protein interactions and quaternary structure of two or more proteins in a sample comprising: adding to the sample a mixture of different amino acid-specific Conversome molecules of Embodiment 47, wherein at least two intact proteins in a natural state are actively interacting; binding the mixture to accessible cognate amino acids on each interacting protein; treating the boundmixture with a concatenating agent such that single-stranded cis-Decodon, complementary single-stranded trans-Decodon, or double-stranded cis- and trans-Decodon strands are concatenated to form at least a concatenated pDNA strand representing the interacting proteins in their natural state; treating under denaturing conditions to separate concatenated pDNA strand(s) from bound Conversome molecules; and detecting the concatenated pDNA sequences by qPCR, next-generation sequencing, or other method.[000494] Embodiment 120. A process for detecting the presence of modified amino acid(s) in a protein sample comprising: treating a sample containing a mixture of proteins suspected of having one or more modified amino acids under denaturing conditions to form unfolded protein sequences; adding to each unfolded mixture a mixture of different amino acid-specific Conversome molecules and one or more modified amino acid-specific Conversome molecules; binding the specific and modified-specific Conversome molecules to controls and suspect sequences, respectively; treating the bound Decodon elements with a concatenating agent to form pDNA strand(s) representing the sequences having one or more modified amino acids; treating under denaturing conditions to release each concatenated pDNA strand; and detecting the presence or absence of a modified amino acid by sequencing the released concatenated pDNA strands or by qPCR.[000495] Embodiment 121. A process for detection of at least two different specific amino acids on a polypeptide strand in a sample using a modified specific Conversome molecule comprising: modifying the Ligamer element of a first Conversome molecule so that the Ligamer comprises at least two different amino acid recognition portions for binding to at least two corresponding adjacent cognate amino acids on the unfolded polypeptide; adding a mixture of different specific Conversome molecules including modified specific Conversome molecules; binding to accessible cognate amino acids; adding a ligase or another concatenation agent; concatenating the Decodon elements of the bound specific and modified specific Conversome molecules to form a pDNA sequence representing the amino acid sequence; denaturing to separate each concatenated pDNA strand from the bound Conversome molecules; and detecting the at least two different specific amino acids based on the concatenated sequence.[000496] Embodiment 122. The process of any of Embodiments 105-121, wherein the Conversome molecule's Ligamer element recognizes two or more cognate amino acids in a protein molecule.[000497] Embodiment 123. The process of Embodiment 122, wherein a protein sequence is detected without pre-linking Conversome molecules by: adding a mixture of different specific Conversome molecules to the unfolded polypeptide sequence, wherein the Decodon cis-Decodon strands are single-stranded; binding the plurality to their specificcognate amino acids; adding a specific labeled targeting oligonucleotide strand to the solution containing the bound mixture; and detecting the protein sequence via a fluor or an enriched immunoprecipitation assay based on hybridization of the labeled targeting oligo to complementary consecutive Decodon pDNA strands.[000498] Embodiment 124. The process of any of Embodiments 105-121 and 123, wherein the specific Decodon strands have at least one or both strands comprising at least one end or both of a 5' and 3' end modified with one or more of: a blocking molecule on either the 5' or 3' end of one cis- or trans-Decodon strand with an OH or a PO4 on the opposite end and the complementary strand with the corresponding OH or PO4 on the opposite complementary end; lacking a 3' OH on both complementary ends of the cis- and trans-Decodon strands with OH and PO4 molecules on opposite complementary ends; a PO4 at each 5' or 3' end of the double-stranded Decodon with an OH at each opposite end of the complementary strand; and the double-stranded Decodon with neither OH nor PO4 on both ends of one strand and OH and PO4 on opposite ends of the complementary strand.[000499] Embodiment 125. The process of any of Embodiments 105-121 and 123-124, wherein at one or both Decodon strand ends is at least one of: blunt end, 1-10 base 5' overhang, 1-10 base 3' overhang, 15-base overhang, 20-base overhang, 25-base overhang, 30-base overhang, and 35-base overhang at either or both of the 5' and 3' ends.[000500] Embodiment 126. A process for detecting the presence or absence of at least one specific protein in a sample containing a mixture of proteins, or distinguishing between two or more different proteins in the sample using the OligoConversome molecules of Embodiment 77, wherein the process comprises: pre-linking two or more specific Conversome molecules by concatenating their double-stranded Decodon elements to form pre-linked OligoConversome molecules by concatenating at least cis-to-cis Decodon, trans-to-trans Decodon, or both cis-to-cis and trans-to-trans Decodon strands; denaturing the protein sample to form unfolded polypeptide sequences; adding a mixture of amino acid-specific OligoConversome molecules with pre-linked Decodon elements to the unfolded polypeptide sequences; concatenating the pre-linked Decodon element strands to form concatenated pDNA or pRNA strands representing unfolded polypeptide sequences; releasing and denaturing the concatenated strands; and using the released concatenated strands to detect and / or identify at least one specific protein in the sample or distinguish between two or more different proteins.[000501] Embodiment 127. The process of Embodiment 126, further comprising optionally adding identical non-specific Conversome molecules to bind to unbound amino acids, wherein either cis-to-cis, trans-to-trans, or both cis-to-cis and trans-to-transconcatenation occurs between the non-specific Conversome molecules and the specific Conversome molecules' Decodon strands to fill in gaps of unbound amino acids along the unfolded polypeptide sequences.[000502] Embodiment 128. The process of Embodiment 126, wherein at least two, three, or more Conversome Decodon element oligonucleotide sequences are pre-linked by concatenation.[000503] Embodiment 129. The process of Embodiment 128, wherein each of the two, three, or more pre-linked Decodon element sequences' corresponding Ligamers' one, two, or three amino acid recognition portions each bind to their cognate amino acid occurring as consecutive amino acids on the unfolded polypeptide sequences.[000504] Embodiment 130. The process of Embodiment 129, wherein at least two or three pre-linked Conversome molecules forming an OligoConversome bind to two or three adjacent amino acids on the unfolded polypeptide sequences.[000505] Embodiment 131. The process of Embodiment 130, wherein the first ends of the adjacent pre-linked OligoConversome OligoDecodon strand(s) are concatenated together by a single strand in double-stranded first ends.[000506] Embodiment 132. The process of Embodiment 126, wherein at least a first of at least two pre-linked OligoConversome molecules binds to a first of two adjacent cognate amino acids and at least a second of at least two pre-linked Conversome molecules binds to a second of two adjacent cognate amino acids in an interlocking spatial alignment to the first two adjacent cognate amino acids on the unfolded polypeptide sequence, followed by concatenation of the OligoDecodons of each adjacent pre-linked OligoConversome, wherein a detection molecule comprising at least one of a fluor or enzyme is present, or enrichment is via immunoprecipitation, or capture occurs if a bead is attached to one of the concatenated pDNA sequences.[000507] Embodiment 133. The process of Embodiment 126, wherein at least two prelinked OligoConversome molecules each bind to each of two adjacent cognate amino acids on the unfolded polypeptide sequences; wherein a fluor or bead is attached to one of the pre-linked nucleic acid strands of the OligoDecodon element and detection is by fluor or bead capture of the pDNA sequences.[000508] Embodiment 134. The process of any of Embodiments 105-121, 123-125, and 126, wherein the specific double-stranded Decodon and OligoDecodon strands have at least one or both strands comprising at least one end or both of a 5' and 3' end modified with one or more of: a blocking molecule on either the 5' or 3' end of one cis- or transDecodon or OligoDecodon strand with an OH or a PO4 on the opposite end and thecomplementary strand with the corresponding OH or PO4 on the opposite complementary end; lacking a 3' OH on both complementary ends with OH and PO4 on opposite complementary ends; a PO4 at each 5' or 3' end with OH at each opposite complementary end; and with neither OH nor PO4 on both ends of one strand and OH and PO4 on opposite ends of the complementary strand, for both Decodon and OligoDecodon doublestranded constructs.[000509] Embodiment 135. The process of Embodiment 131, wherein the OligoDecodon elements' OligoDecodon strand(s) are concatenated together by the first complementary trans-Decodon strand.[000510] Embodiment 136. A kit for determining the amino acid sequence of a protein molecule comprising: a plurality of a mixture of specific Conversome molecules for each of 20 proteinogenic amino acids exclusive of selenocysteine and pyrrolysine; or 20 vials of specific Conversome molecules, one vial for each specific proteinogenic amino acid; optionally a limited number of vials with mixtures of specific proteinogenic amino acids; T4 DNA ligase; optionally at least one vial each of specific Conversome molecules for selenocysteine and pyrrolysine; optionally at least one vial of a plurality of one non-specific Conversome molecule; and instructions for use of the specific and non-specific Conversome molecules; wherein specific Decodon elements for each of the 20 proteinogenic amino acids and one non-specific Decodon element each comprise specific and non-specific Decodon strands comprising oligonucleotide nucleic acid sequences.[000511] Embodiment 137. The kit of Embodiment 136, wherein each of the specific and non-specific Decodon strand oligonucleotide sequences is from 2 to 300 nucleic acids in length and selected from DNA, RNA, LNA, PNA, TNA, GNA, HNA, CeNA, and FANA.[000512] Embodiment 138. The kit of Embodiment 137, wherein each of the specific and non-specific Decodon oligonucleotide sequences is a single-stranded cis-Decodon.[000513] Embodiment 139. The kit of Embodiment 137, wherein each of the specific and non-specific Decodon oligonucleotide sequences is a double-stranded cis- and complementary trans-Decodon.[000514] Embodiment 140. The kit of Embodiment 138, wherein the single-stranded cis-Decodon further comprises at least one blocked 5' and / or 3' end.[000515] Embodiment 141. The kit of Embodiment 139, wherein the double-stranded cis- and complementary trans-Decodon further comprises at least one blocked 5' and / or 3' end.[000516] Embodiment 142. The kit of Embodiments 139 and 140, wherein the blocked 5' and / or 3' end is selected from a detection molecule on one end of the cis-Decodon or on one end of one strand of the double-stranded cis- or trans-Decodon, a hydrogen on each end of the cis-Decodon or on each end of one strand of the double-stranded cis- or trans-Decodon, and a hydrogen at one end of both complementary ends of the two doublestranded cis- and trans-Decodon strands; wherein the end with the detection molecule or hydrogen(s) is blocked from concatenation with adjacent or proximal Conversome Decodon elements' single-stranded cis-Decodon or at least one strand of double-stranded cis- and trans-Decodon oligonucleotide sequences.[000517] Embodiment 143. An accessory kit for determining the amino acid sequence of a protein molecule comprising: at least one vial of a plurality of one non-specific Conversome molecule; T4 DNA ligase; and instructions and methods for use.[000518] Embodiment 144. The kit of Embodiment 143, wherein the non-specific Conversome molecule further comprises a Decodon element whose oligonucleotide sequence is a single-stranded cis-Decodon.[000519] Embodiment 145. The kit of Embodiment 143, wherein the non-specific Conversome molecule further comprises a Decodon element whose oligonucleotide sequences are double-stranded cis- and complementary trans-Decodon.[000520] Embodiment 146. A kit for determining the amino acid sequence of a protein molecule comprising: a plurality of a mixture of at least two or more specific Conversome molecules for each proteinogenic amino acid, or vials of Conversome molecules with at least two specific Conversome molecules pre-linked by their respective Decodon oligonucleotide sequence(s) prior to binding to their respective cognate amino acids forming OligoConversome molecules; T4 DNA ligase; instructions and methods for use of non-specific Conversome molecules with OligoConversome molecules; optionally at least one vial of a plurality of one non-specific Conversome molecule; and instructions for use of the pre-linked specific OligoConversome molecules and non-specific Conversome molecules; wherein specific OligoDecodon elements for each of the 20 proteinogenic amino acids and one non-specific Decodon element each comprise either specific OligoDecodon strands or non-specific Decodon strands comprising oligonucleotide sequences.[000521] Embodiment 147. The kit of Embodiment 146, wherein each of the specific OligoDecodon strand and non-specific Decodon strand oligonucleotide sequences are single-stranded cis-OligoDecodon and non-specific cis-Decodon strands, respectively.[000522] Embodiment 148. The kit of Embodiment 146, wherein each of the specific OligoDecodon and non-specific Decodon oligonucleotide sequences are double-stranded cis- and complementary trans-OligoDecodon strands and double-stranded cis- and complementary trans-Decodon strands, respectively.EXAMPLES[000523] The following examples are provided for illustrative purposes only and not to limit the scope of the claims provided herein.[000524] Example 1 Construction of a Conversome™ molecule[000525] The purpose of this example is to provide a method of synthesis of a Conversome molecule for a specific proteinogenic amino acid. The method of synthesis can be adapted for each amino acid family’s classification(s) based on functional groups and the Decodon sequence uniquely specific for any amino acid type.[000526] Ligamer End:[000527] The following assembly of a Conversome molecule uses RNA bases:[000528] 5’-Hexynyl- GACGAGAAGGAGCGCUGGUUCUACUAGCAGGUAGGUCACUCGUC-3’[000529] (SEQ ID NO:1). This will result in the creation of an Arginine specific Conversome molecule.[000530] Hexynyl creates a 5' terminal alkyne group which reacts with azides in the presence of copper (I) to form stable 1 ,2,3-triazole bonds (termed Click reaction).[000531] Decodon End:[000532] The Decodon sequence is: 5'-CTGG-Azide-CTGC-3' (SEQ ID NO:2)[000533] The Azide is placed at position 4 in the Decodon sequence which is 9 nucleotides in length.[000534] A Modification is attached to the oligo through a dT base (not in SEQ ID NO:2).[000535] The Azide modifications use an NHS Ester functional group to attach an azide moiety in an oligo. This azide moiety may subsequently be used to attach alkyne modified groups through the click reaction.[000536] Click Reaction Protocol to Assemble a specific Conversome molecule consists of:[000537] 1. Dissolve the Ligamer element in 1 ml vial, sterile, deionized water in a pressure-tight vial to 2 uM. Starting concentration will be 100 uM;[000538] 2. Add 1M triethylammonium acetate buffer, pH 7.0 to 0.2M;[000539] 3. Add DMSO to 50%, and vortex;[000540] 4. Add azide Decodon stock solution (3uM in DMSO), and vortex; Note: The Azide Decodon stock solution comprises Azide (iAzideN) at different positions in the Decodon (N = oligonucleotide, A, T, G or C for DNA nucleic acids or A, II, G or C for RNA nucleic acids). Azide modifications use an NHS Ester functional group to attach an azide moiety at the 5', 3' or any internal position in an oligo. This azide moiety may subsequently be used to attach alkyne modified groups through the click reaction as is known to one of skill in the art.[000541] 5. Add 99% Ascorbic Acid Stock solution to the mixture to 0.5mM, and vortex briefly;[000542] 6. Degas the solution by bubbling inert gas in it for 30 seconds. Nitrogen, argon, or helium gas can be used;[000543] 7. Add Copper (ll)-TBTA Stock (10mM) in 55% DMSO to the mixture to 0.5mM. Flush the vial with inert gas and close the cap;[000544] 8. Vortex the mixture thoroughly. If significant precipitation of azide is observed; heat the vial for 3 minutes at 80°C, and vortex;[000545] 9. Keep at room temperature overnight;[000546] 10. Add at least 4-fold volume of acetone (Pharmaceutical grade) to the mixture. Mix thoroughly and keep at -20°C for 20 minutes, followed by;[000547] 11. Centrifuging at 18°C (room temperature), 10000 rpm for 10 minutes;[000548] 12. Discard the supernatant;[000549] 13. Wash the pellet with acetone (1 mL), centrifuge at 18°C (room temperature), 10000 rpm for 10 minutes;[000550] 14. Discard the supernatant, dry the pellet, and purify the conjugate by RP- HPLC or PAGE.[000551] The resulting Arg Conversome molecule specifically binds to Arginine amino acids in any protein or polypeptide sequence. Adapted from PubMed entry PMID:10769757.[000552] Example 2 Identification of new proteins within a mixture of other proteins[000553] This experiment illustrates the use of Conversome molecules for discovery and / or to identify foreign, invasive organism(s) proteins, in a background of a collection of known proteins’ amino acid sequences.[000554] The bacteria in and on our bodies make thousands of tiny, previously unidentified proteins that could shed light on human health and advance drug development. See, e.g., Cell (2019), article identifier S0092-8674(19)30781-0. These could be identified by using Conversion methods wherein a protein molecule(s) amino acid sequence(s) is converted to pDNA for further identification and / or analyses by qPCR.[000555] New Al system designs proteins that successfully bind to target molecules, with potential for advancing drug design, disease understanding and more. Article identifier arXiv:2409.08022. These proteins could be quantitated with Conversion even though there are no antibodies to them.[000556] By nature, proteins are highly complex. Therefore, as a consequence of the dynamic range and sensitivity limits of current proteomic techniques, many predicted protein products have not yet been identified in proteomic experiments. These proteins could provide essential clues to aid interpretation of biological processes and potentially drive new avenues of research and therapeutic strategies to solve remaining clinical problems. As a consequence of the high diversity of individuals, it is crucial to perform large-scale analyses of clinical samples. This enables the identification of the highest number of proteins possible, including proteins that have never been previously reported by mass spectrometry. In the current study, a novel data set of 33 proteins is presented. These proteins were identified across 140 lymph node metastatic tumour samples from malignant melanoma patients. NCBI identifier: PMC7320927.[000557] Example 2 Construction of an OligoConversome™ molecule[000558] The purpose of this example is to provide a method of synthesis of an OligoConversome molecule for a specific proteinogenic amino acid. The method of synthesis can be adapted for each amino acid family’s classification(s) based on functional groups and the Decodon sequence uniquely specific for any amino acid type.[000559] Position 1 Ligamer End:[000560] The following assembly of an OligoConversome molecule uses RNA bases:[000561] 5’-Hexynyl-GACGAGAAGGAGCGCUGGUUCUACUAGCAGGUAGGUCACUCGUC-3’[000562] (SEQ ID NO:1)[000563] Hexynyl creates a 5' terminal alkyne group which reacts with azides in the presence of copper (I) to form stable 1 ,2,3-triazole bonds (termed Click reaction).[000564] Position 1 Decodon End:[000565] The Decodon sequence is: 5'-CTGG-Azide-CTGC-3' (SEQ ID NO:2)[000566] The Azide is placed at position 5 in the Decodon sequence which is 9 nucleotides in length.[000567] A Modification is attached to the oligo through a dT base (not in SEQ ID NO:2).[000568] The Azide modifications use an NHS Ester functional group to attach an azide moiety in an oligo. This azide moiety may subsequently be used to attach alkyne modified groups through the click reaction.[000569] Click Reaction Protocol to Assemble a specific Conversome molecule consists of:[000570] 1. Dissolve the Ligamer element in water in a pressure-tight vial to 2 uM;[000571] 2. Add triethylammonium acetate buffer, pH 7.0 to 0.2M;[000572] 3. Add DMSO to 50%, and vortex;[000573] 4. Add azide Decodon stock solution (3uM in DMSO), and vortex;.[000574] 5. Add Ascorbic Acid Stock solution to the mixture to 0.5mM, and vortex briefly;[000575] 6. Degas the solution by bubbling inert gas in it for 30 seconds. Nitrogen, argon, or helium gas can be used;[000576] 7. Add Copper (ll)-TBTA Stock in 55% DMSO to the mixture to 0.5mM. Flush the vial with inert gas and close the cap;[000577] 8. Vortex the mixture thoroughly. If significant precipitation of azide is observed; heat the vial for 3 minutes at 80°C, and vortex;[000578] 9. Keep at room temperature overnight;[000579] 10. Add at least 4-fold volume of acetone to the mixture. Mix thoroughly and keep at -20°C for 20 minutes, followed by[000580] 11. Centrifuging at 10000 rpm for 10 minutes;[000581] 12. Discard the supernatant;[000582] 13. Wash the pellet with acetone (1 mL), centrifuge at 10000 rpm for 10 minutes;[000583] 14. Discard the supernatant, dry the pellet, and purify the conjugate by RP- HPLC or PAGE.[000584] The resulting OligoConversome molecule specifically binds to Arginine amino acids in any protein or polypeptide sequence.[000585] Position 2 Ligamer End:[000586] The following assembly of a Conversome molecule uses RNA bases:[000587] 5’-Hexynyl- GACGAGAAGGAGCGCUGGUUCUACUAGCAGGUAGGUCACUCGUC-3’[000588] (SEQ ID NO: 1)[000589] Position 2 Decodon End:[000590] The Decodon sequence is: 5'-AGCC-Azide-CGTA-3' (SEQ ID NO: 4)[000591] Follow above example for synthesis starting at paragraph

[0427] to

[0254] the Protocol to Assemble a specific Conversome molecule consists of: Steps 1 - 14, below)[000592] The resulting Position 2 Conversome molecule specifically binds to Tyrosine amino acids in any protein or polypeptide sequence.[000593] Position 3 Ligamer End:[000594] The following assembly of a Conversome molecule uses DNA bases:[000595] 5’-Hexynyl- GCGCTGGAGCTTGGATTGATGTGGTGTGTGAGTGCGGTGCCCAGC-3’[000596] (SEQ ID NO: 7)[000597] Position 3 Decodon End:[000598] The Decodon sequence is: 5'-CTAG-Azide-GCGA-3' (SEQ ID NO:5)[000599] Follow above example for synthesis starting at paragraph

[0012] [000600] The resulting Position 3 Conversome molecule specifically binds to Tyrosine amino acids in any protein or polypeptide sequence.[000601] OligoConversome Assembly:[000602] 1. A trans-Decodon made of an oligonucleotide of sequence 5'- TCGCACTAGTACGAGGCTGCAGACCAG-3' (SEQ ID NO:6) is dissolved to 10nM in analytical grade DNase / RNase free water[000603] 2. The three Conversomes (Position 1, Position 2 and Position 3) are dissolved in 10mM Tris pH 8.0 to a concentration of 100nM[000604] 3. The Conversomes are added to the trans-Decodon in equal volumes making the concentrations 2.5nM for the trans-Decodon and 25nM for each of the Conversomes[000605] 4. The reaction is heated to 50 degrees and then cooled to 18 degrees at a rate of 1 degree per 10 seconds[000606] 5. Purify the assembled OligoConversome by RP-HPLC or PAGE.[000607] The resulting Conversome molecule specifically binds to an amino acid sequence of Arginine-Tyrosine-Arginine in any protein or polypeptide sequence.[000608] Example 3 Identification of new proteins within a mixture of other proteins [000609] This experiment illustrates the use of Conversome molecules to discovery and / or identify foreign, invasive organism(s) proteins, in a background of a collection known proteins’ amino acid sequences.[000610] The bacteria in and on our bodies make thousands of tiny, previously unidentified proteins that could shed light on human health and advance drug development. See, e.g., Cell (2019), article identifier S0092-8674(19)30781-0. These could be identified by using Conversion methods wherein a protein molecule(s) amino acid sequence(s) is converted to pDNA for further identification and / or analyses by qPCR.[000611] New Al system designs proteins that successfully bind to target molecules, with potential for advancing drug design, disease understanding and more. Article identifier arXiv:2409.08022. These proteins could be quantitated with Conversion even though there are no antibodies to them[000612] By nature, proteins are highly complex. Therefore, as a consequence of the dynamic range and sensitivity limits of current proteomic techniques, many predicted protein products have not yet been identified in proteomic experiments. These proteins could provide essential clues to aid interpretation of biological processes and potentially drive new avenues of research and therapeutic strategies to solve remaining clinical problems. As a consequence of the high diversity of individuals, it is crucial to perform large-scale analyses of clinical samples. This enables the identification of the highest number of proteins possible, including proteins that have never been previously reported by mass spectrometry. In the current study, a novel data set of 33 proteins is presented. These proteins were identified across 140 lymph node metastatic tumour samples from malignant melanoma patients. NCBI identifier: PMC7320927.[000613] Example 4 Quantitation of a Protein Within a Protein Mixture[000614] p53 protein levels are tightly regulated and vary depending on the cell's environment (high in cancer). NCBI identifier: NBK6412.[000615] After transfection with an mRNA vaccine (may have sequence changes) expression of the protein may not be recognized by the normal antibody giving a false negative. By using Conversomes targeted to the different amino acids, these proteins could be detected during mRNA vaccine screening.[000616] Example 5 Differential Expression of Many Different Proteins To Get a “Signature” of a Sample.[000617] Proteomic signatures improve risk prediction for common and rare diseases Carrasco-Zanini, J., Pietzner, M., Davitte, J., et al., “Proteomic signatures improve risk prediction for common and rare diseases,” Nat Med 30, 2489-2498 (2024).[000618] Proteome changes based on Cell size and growth rate using Mass Spec, more proteins could be analyzed with Conversion. See., e.g., Front Cell Dev Biol. 2022 Sep 5; 10:980721.[000619] Undulating changes in human plasma proteome profiles across the lifespan with age-related molecular changes in blood could provide new insights into age-related disease biology. See, e.g., Nature Medicine volume 25, pagesl 843-1850 (2019).[000620] Understanding COVID-19 progression with longitudinal peripheral blood mononuclear cell proteomics: Changes in the cellular proteome over time emphasizes the significance of longitudinal cellular proteomic studies in identifying disease progression-related pathways and persistent protein changes post-hospitalization. See, e.g., Understanding COVID-19 progression with longitudinal peripheral blood mononuclear cell proteomics: Changes in the cellular proteome overtime. Figueiredo Leite, Giuseppe Gianini etal. iScience, Volume 26, Issue 10, 107824[000621] An exemplary illustration of the results of Proteome Analyses from 50 patients is found in Figure 18.[000622] Example 6 Detection of alternatively spliced proteins[000623] The loss of the nuclear localization signal (NLS) in the sex-determining region Y protein (SRY) has been shown to be associated with XY sex reversal in Swyer syndrome.[000624] Example 7 Protein localization within a body[000625] CRP (C-reactive Protein) rises in the blood in response to inflammation and infection. See NCBI identifier: NBK430685.[000626] Cardiac Troponins are released into the bloodstream when heart muscle is damaged. Monitoring a large number of these would be possible. See NCBI identifier: PMC5852618.[000627] Example 8 Detection of Post-Translational Protein Modifications (Protein Cleavage)[000628] Proteolytic cleavage of proproteins into active forms (e.g., TGF-b activation after cleavage promoting growth and differentiation) can be missed with antibodies, if multiple regions are targeted, then protein cleavage can be quantitated. See NCBI identifier: 18243766.[000629] Protein cleavage may leave a nonfunctional protein that is recognized by an antibody, Using Conversomes multiple sites within each protein can be targeted.[000630] Example 9 Detection of Translational Mistakes[000631] Misincorporation of amino acids.[000632] Frameshift errors with cystic fibrosis and Duchenne MS.[000633] Ribosomal pausing e.g., ALS caused by RNA misfolding and in Huntington’s disease ribosomes move slowly allowing proteins to misfold.[000634] Example 10 Determine 3D structure of a protein[000635] Prions are proteins that have misfolded and can cause other proteins to misfold as well. The term "prion" comes from "proteinaceous infectious particle".Conversomes could recognize the different 3D structures of proteins. See, e.g., Nat Commun, 13: Article S41467-022-31460-8 (2022). The disclosed compositions and methods can be used in elucidating various 3E structures of proteins as illustrated in Figure 12A-12E.[000636] Example 11 Determination / detection of protein:protein interactions [000637] During initiations of DNA replication multiple proteins are assembled together (the preinitiation complex, six ORC proteins (ORC1-6), Cdc6, Cdt1, and a heterohexamer of the six MCM proteins (MCM2-7). The disclosed compositions and methods can be used in identifying protein interactions to facilitate protein assembly as illustrated in Figure 13A-13F, 16A-16F.[000638] Example 12 Detection of Post-Translational Protein Modifications (Amino Acid Modifications)[000639] Estrogen receptor a (ER- a) is phosphorylated at many different positions and phospho-profiling of ER-a in human breast tumors to establish an ‘ER-a phosphorylation code’, may be a more accurate marker of prognosis and / or response to endocrine therapy in human breast cancer. The disclosed compositions and methods can be used in phosphor-profiling of the ER as illustrated in Figures 14A-14E.[000640] Example 13 Determination, Disease Detection and Data Analysis of Protein Quantity in Normal vs. Diseased Samples, Protein Isoform Analysis[000641] The disclosed invention will be able to distinguish protein isoforms using OligoConversomes and qPCR. As depicted in the bar charts of FIG. 17, Isoform 1 is associated with normal conditions. Isoform 2 is linked to disease. When testing at progressive time points the following analyses of the protein isoforms show that at:[000642] Time Point 1 : At initial diagnosis- There is a preponderance of normal samples that predominantly contain protein Isoform 1. The Diseased samples show a near 1:1 ratio of Isoform 1 to Isoform 2.[000643] Time Point 2: Indicating disease progression- The Normal samples continue to show a dominance of Isoform 1. The Diseased samples exhibit a significant increase in Isoform 2 relative to Isoform 1. The increasing quantities of Isoform 2 provides confirmation of a progressing diseased state correlating with increasing Isoform 2 levels.[000644] Time Point 3: Following treatment- Therapeutic intervention impacts a positive effect as the treated diseased samples will show an increase in Isoform 1, suggesting treatment effectiveness in reducing Isoform 2 levels. The disclosed compositions and methods can be used in elucidating various quantity of proteins in Normal vs. Diseased samples of proteins and / or protein isoforms as illustrated in Figure 17 (isoforms) and Figures 12A-12E (secondary and tertiary structures).[000645] Example 14 Determination Disease Detection and Data Analysis of Protein Quantity in Normal vs. Diseased Samples, Analyzing Proteome Expression Patterns [000646] The disclosed invention will be able to analyze proteome expression patterns using Next Generation Sequencing of pDNA. As depicted in the cluster mapping of protein expression profiles of FIG. 18, 50 patients’ proteomes have varying levels and similar proteins are showing similar expressions.[000647] The analysis includes 50 patients, with each sample to be measured in duplicate and combined before plotting. Each data point represents a quantitative measurement of protein expression profiles obtained through sequencing. In this visualization, the data points are clustered using Uniform Manifold Approximation andProjection (LIMAP) to capture similarities between the patients based on their proteome profiles. Samples with similar protein expressions are grouped closer together, enabling the identification of patterns or differences across the dataset. For instance, "Sample I Profile 1" and "Sample I Profile 2" display a higher degree of similarity in their protein profiles, clustering closely together, whereas "Sample I Profile 6" stands apart, indicating unique protein expressions that differentiate it from the other patients. This distinction could be attributed to specific proteins uniquely expressed in "Sample I Profile 6." The Conversome molecules can be used to identify protein expression patterns in a patient population but will provide predictive analytics of both immediate, interim, and long-term disease conditions, risks and projections. Prophetic results obtained with utilizing Conversome molecule in Proteome profiling of a collective of patients are illustrated in Figure 18.[000648] Example 15: Conversome Purification and Quality Control[000649] Objective. To assemble and purify high-purity Conversomes with and demonstrate their use in peptide-dependent concatenation (FIG. 20A-20F).[000650] FIG. 20A is a schematic depicting modular assembly of Conversomes by copper-catalyzed azide-alkyne cycloaddition (CuAAC) or strain-promoted azide-alkyne cycloaddition (SPAAC). Ligamer(s) are conjugated to Decodon tag(s) through a tetraethylene glycol (TEG) linker to provide spatial flexibility and aqueous solubility. CisDecodons may incorporate azides at the 3' end, 5' end, and / or internally to enable single-or multi-Ligamer configurations. The arrangement permits positioning of one or more Ligamers per Decodon to support mono- or bispecific designs while preserving downstream concatenation compatibility.[000651] FIG. 20B is an exemplary build showing Ligamer-Decodon connectivity for amino-acid-specific exemplary Conversomes. FIG. 20B Left: Arg-specific Conversome with Arg Ligamer coupled to left and right Decodon elements at designated linkage sites. Right: Ser-specific Conversome with Ser Ligamer similarly coupled to matched Decodons. Each construct uses defined azide / DBCO handles on Decodons and complementary click handles on Ligamers to control orientation, valency, and placement, enabling consistent interlocking spatial alignment for concatenation.[000652] Materials and Methods. Ligamer and Decodon components were synthesized as described in Examples 1-2. Click-conjugation was performed in aqueous copper-free solution buffers. Reaction conditions were screened to modulate molar ratios of LigamerDecodon and reaction time to deplete single-Ligamer intermediates. The crude reaction mixture was fractionated and observed through gel, with all species ofConversomes reactions components observable. The distinct band patterns reflect Conversome assembly efficiency under various reaction conditions (FIG. 20C).[000653] Fractions were analyzed by 15% denaturing urea PAGE (FIG. 20E). Bands corresponding to free Ligamer, single-Ligamer Conversomes, and full Conversomes were identified by migration profiles relative to synthetic standards and spiked markers. The crude reaction was HPLC purified for full Conversome species.[000654] Results. HPLC resolved three predominant peaks assignable to free Ligamer, single-Ligamer Conversome, and full Conversome species (FIG. 20D). Denaturing PAGE confirmed removal of free Ligamer and single-Ligamer species in the pooled “full Conversome” fractions (FIG. 20E). The purified Conversomes displayed robust performance in downstream ligation reactions, yielding higher peptide-dependent pDNA signals and lower off-target background relative to unfractionated materials (not shown). Bispecific Conversomes carrying two Ligamers and a single Decodon were assembled, purified and similarly evaluated via denaturing PAGE and HPLC (FIG. 20F).[000655] Conclusion. Assembly and purification conditions yield functional both monoamino acid specific and / or bispecific multi-Ligamer Conversomes at high purity with depleted non-productive species, supporting downstream peptide-dependent pDNA generation.[000656] Example 16: Ligation-Based Conversion and qPCR Readout.[000657] Objective. To demonstrate peptide-dependent pDNA formation using ligase-mediated Decodon concatenation and qPCR detection.[000658] Materials and Methods. Purified Conversomes specific for user-selected amino acids were incubated with a denatured target peptide (conjugated to bead) in a buffered solution containing Mg2+ and non-ionic detergent (schematic in FIG. 21A).[000659] Following binding, a DNA ligase was added with ATP and crowding agents to facilitate concatenation of adjacent Decodon strands. Post-concatenation, the magnetic bead with peptide dependent pDNA products were washed to rid of background products. The magnetic bead with peptide-template and pDNA is added to qPCR reactions. The qPCR primers were designed to constant regions flanking Decodon junctions; SYBR green assay was used for pDNA signal detection with options of designing a hydrolysis probe targeting concatenation junctions of fully assembled pDNA. Control reactions included: (i) trans-Decodon only (no Ligamers), (ii) peptide-independent supernatant, and (iii) negative no-ligase control. FIG. 21 B is a generalized schematic for the executed peptide-dependent pDNA formation: purified Conversomes were incubated with denatured peptide / protein to allow Ligamer binding. A DNA ligase with ATP and crowding agents were added toconcatenate adjacent Decodon strands upon reaching an interlocking spatial alignment. Concatenated peptide dependent pDNA that is associated with the peptide and beads are washed to get rid of background products. The pDNA that is peptide bound is then detected by qPCR. Controls include trans-Decodon-only, peptide-independent supernatant, and no-ligase conditions.[000660] Results. Robust amplification was observed exclusively in peptide-dependent reactions, with substantially delayed Cq in trans-Decodon-only and peptide-independent controls. The assay design supports both singleplex and multiplex qPCR, and is compatible with downstream NGS library preparation from the same eluates (FIG. 21 B, workflow schematic).[000661] Conclusion. Ligase-mediated concatenation of Decodon strands yields sequence-specific pDNA detectable by qPCR with favorable signal-to-background properties in peptide-dependent conditions (FIG22A and FIG22B).[000662] FIG. 22A shows titration of histidine specific Conversome with against a histidine peptide and a histidine-negative peptide. The pDNA signal by qPCR positively correlates with histidine peptide only, indicating histidine specific Conversome mediated pDNA signal is histidine containing peptide dependent. FIG. 22B shows Ligase-mediated concatenation of Decodon strands yields sequence-specific pDNA detectable by qPCR with favorable signal-to-background properties in peptide-dependent conditions in various sequence combinations.[000663] Example 17: Peptide-Dependent Full-Length pDNA Sequencing (SS-RR-WW (SEQ ID NO: 12))[000664] Objective. To validate full-length pDNA corresponding to a defined peptide motif using Oxford Nanopore long-read sequencing and mapping.[000665] Materials and Methods. Conversomes recognizing Ser (S), Arg (R), and Trp (W) were combined with a peptide comprising SS-RR-VWV (SEQ ID NO: 12). After binding, trans- and / or cis-mediated Decodon concatenation was performed as described herein. pDNA was prepared for ONT sequencing using ligation-based library prep.Sequencing data were basecalled and mapped to the expected pDNA reference corresponding to the SS-RR-WW (SEQ ID NO: 12) motif. Controls included transDecodon only processed identically, and a peptide-independent supernatant. A portion of the eluate was also reserved for Illumina-compatible library prep.[000666] Results. In FIG. 22C, alignment tracks in IGV showed canonical Decodon tracts consistent with the expected residue order; representative tracks displayed the Ser, Arg, and Trp identifiers at the appropriate positions. Included internally the pDNAsequences are two barcoded tags “TTAC” and “CACA”, where unique molecular identifiers may be incorporated. Full-length pDNA mapping occurred at significantly higher frequency in the peptide-dependent reaction (21.6%) than in trans-Decodon only (6.7%) and peptide-independent supernatant (8.5%) (FIG. 22D, mapping summary).[000667] Conclusion. The SS-RR-WW (SEQ ID NO: 12) model peptide yields a sequence-accurate, full-length pDNA product with markedly enriched mapping relative to controls, establishing peptide dependence and validating the conversion chemistry with nanopore sequencing.[000668] FIG. 22E (SEQ ID Nos: 14-36) demonstrates the designing of an oligoConversome targeting Estrogen Receptor alpha (ESR1). The targeted protein ESRTs sequence was broken down into short fragments and mapped back to protein reference database for uniqueness. Regions of ESR1 that is unique were identified for oligoConversome design as a target site. Two oligoConversomes were designed spanning the ESR1 unique sequence region. The pDNA created based on the assay design can be used to identify and quantify ESR1 in the sample.[000669] Example 18: Targeted Multi-Extension and Concatenation Using LAX Domains (Trans and Cis)[000670] Objective. To demonstrate that a short constant “LAX” domains can improve spatial alignment and hybridization specificity for Decodon joining in both trans- and cisextension modes, yielding products that are efficient PCR substrates.[000671] Materials and Methods. Two Conversomes (Conversome 1 and Conversome 2) bearing distinct Ligamers and Decodon sequences were designed with flanking constant LAX domains forming short interlocking motifs FIGs. 23A-D. In trans-extension, complementary trans-Decodons anneal with a top strand (FIGs. 23B) when Ligamers are positioned adjacently on the peptide, and ligase or polymerase-nick sealing completes joining (FIGs. 23C-D). In cis-extension, hybridization domains on cis-Decodons guide polymerase-mediated fill-in and nick repair on the opposite strand (not depicted). Reaction conditions are tuned such that LAX domains interact minimally in bulk but form stable alignments upon peptide-induced spatial alignment. Products can be amplified with universal primers annealing to constant regions.[000672] Results. In both trans and cis modes, incorporation of LAX domains increases the proportion of correctly joined products and reduced background concatenation in peptide-absent controls(not shown).[000673] Conclusion. LAX domains facilitate peptide-dependent interlocking spatial alignment joining of Decodon strands by enhancing local hybridization, thereby improving specificity and yield of intended pDNA products.[000674] Example 19: Affinity Enrichment and Bead-Based Workflows[000675] Objective. To enable sensitive enrichment of targeted protein in a mixture by coupling Conversomes to magnetic-bead capture.[000676] Materials and Methods. A mixture of dye-conjugated peptides was combined with Conversomes (specific for a target peptide) hybridized to a biotinylated TransDecodon. The mixture was incubated with streptavidin beads, followed by washing and elution (FIG. 24A) (SEQ ID Nos: 37-40). The eluted peptides was analyzed by HPLC to distinguish peptide species based on retention time (fractions) and end-point read for quantity by qPCR instrument.[000677] Results. The target specific Conversome successfully enriched the target peptide in a mixture with high purity (FIG. 24B) (SEQ ID Nos: 11, 37 and 59).[000678] Conclusion. Demonstrated that Conversome mediated affinity-based capture can enrich target peptides in a background of mixtures with high purity.[000679] While the principles of this invention have been described in connection with specific embodiments, it should be understood clearly that these descriptions are made only by way of example and are not intended to limit the scope of the invention. What has been disclosed herein has been provided for the purposes of illustration and description. It is not intended to be exhaustive or to limit what is disclosed to the precise forms described. Many modifications and variations will be apparent to the practitioner skilled in the art. What is disclosed was chosen and described in order to best explain the principles and practical application of the disclosed embodiments of the art described, thereby enabling others skilled in the art to understand the various embodiments and various modifications that are suited to the particular use contemplated. It is intended that the scope of what is disclosed be defined by the following claims and their equivalence.[000680]

Claims

1. WHAT IS CLAIMED IS:

1. A composition comprising:a plurality of concatenated monomers, each monomer comprising:a residue-recognition moiety configured to recognize and bind to a residue of an amino acid or a residue of a polypeptide;optionally a linker moiety comprising a first end and a second end, wherein the first end is bonded to the residue recognition moiety; anda residue-labeling moiety comprising a nucleic acid tag comprising at least one nucleotide, wherein the residue-labeling moiety is bonded to the second end of the linker moiety or directly to the residue recognition moiety,and whereby the plurality of concatenated monomers are concatenated at the residue labeling moiety.

2. The composition of claim 1, wherein at least two nucleic acid tags are pre-linked to each other prior to being added into the composition.

3. The composition of claim 1 or 2, further comprising a non-specific residue-tagging monomer whose residue-recognition moiety binds indiscriminately to accessible residues and whose nucleic-acid tag is concatenation-compatible to fill unbound sequence positions.

4. The composition of claim 1 or 2, further comprising a sub-set of residue recognition moiety(ies) configured to recognize and bind to a sub-set of pre-determined residue(s) of an amino acid or a sub-set of pre-determined residue(s) of a polypeptide(s);5. The composition of any of claims 1—4, wherein concatenation is effected enzymatically or chemically, or with a combination thereof.

6. The composition of any of claims 1-5, wherein concatenation is effected via a splint DNA that hybridizes to the plurality of concatenated monomers and extends its sequence via amplification.

7. The composition of any one of claims 1-6, wherein the nucleic-acid tag in the residue labelling moiety is a first oligonucleotide, whereby the second residue labelling moiety is a second oligonucleotide, and whereby the first oligonucleotide and the second oligonucleotide support extension of a nucleic acid sequence when two or more of the plurality of residue tagging monomers in solution reach an interlocking spatial alignment.

8. A composition comprising:a residue-recognition moiety for reversibly or irreversibly binding to a residue of an amino acid or a residue of a polypeptide;optionally a moiety having a first end and a second end, the first end covalently or non-covalently coupled to the residue recognition moiety; anda residue-labeling moiety comprising a nucleic-acid tag coupled to the second end of the linker moiety or directly to the residue recognition moiety, the nucleic acid tag comprising one or more nucleotides.

9. The composition of claim 8, wherein the residue of the amino acid is a natural amino acid residue, selected from proteinogenic, non-proteinogenic, synthetic, or a post-translationally modified amino acid residue.

10. The composition of claim 8, wherein the residue of the polypeptide is selected from proteinogenic, non-proteinogenic, synthetic, in vitro modified, ora post-translationally modified polypeptide residues.

11. The composition of claim 8, wherein the residue-recognition moiety comprises one or more of: an aptamer, oligonucleotide, polypeptide, peptide mimic, nanobody, antibody, antibody fragment, engineered scaffold protein, small-molecule binder, metal-ligand complex, molecularly imprinted polymer, or combinations thereof.

12. The composition of claim 8, wherein the residue-recognition moiety is not an antibody.

13. The composition of claim 8, wherein the residue-recognition moiety reversibly or irreversibly binds to a residue of an amino acid or a residue of a polypeptide.

14. The composition of claim 8, wherein the nucleic-acid tag is selected from the group consisting of: a ribonucleic acid (RNA) nucleotide, a deoxyribonucleic acid (DNA) nucleotide, a locked nucleic acid (LNA) nucleotide, a peptide nucleic acid (PNA) nucleotide, a threose nucleic acid (TNA) nucleotide, a glycol nucleic acid (GNA) nucleotide, a 1,5-anhydrohexitol nucleic acid (HNA) nucleotide, a cyclohexene nucleic acid (CeNA) nucleotide, a fluoroarabino nucleic acid (FANA) nucleotide, and any combination of the foregoing.

15. The composition of claim 8, wherein the nucleic-acid tag has a length from 2 to 500 nucleotides, includes blunt and / or overhang termini, and comprises terminal chemistries selected from phosphate (PO4), hydroxyl (OH), hydrogen (H), ora blocking group.

16. The composition of claim 15, wherein the nucleic acid is single stranded or double stranded.

17. The composition of claim 8, wherein the linker moiety comprises one or more of ethylene glycol, polyethylene glycol, glycerol, aminopurine, carbon spacers, hexanediol, dideoxyribose, photocleavable spacers, melamine, phenolics, dialdehydes, poly(N-(2-hydroxypropyl)methacrylamide), saccharides including alpha-D-glucose, dendrimers including PAMAM dendrimers, sulfonic acid groups, glutathione, poly-L-glutamine, poly-L-glutamic acid, urethane, or combinations thereof.

18. The composition of claim 8, wherein the residue-recognition moiety is configured to bind to two or more residues that are adjacent to one another.

19. The composition of any of claims 8-18, wherein the nucleic-acid tag comprises a first tag strand and a complementary tag strand, and at least one strand includes an end modification limiting concatenation directionality.

20. The composition of claim 19, wherein the nucleic acid tag is a hairpin nucleic acid tag, a double helix nucleic acid tag, or a triple helix nucleic acid tag.

21. The composition of any of claims 8-20, wherein the residue-recognition moiety recognizes at least 2 amino acids that are not juxtaposed into one another.

22. A composition comprising a plurality of residue tagging monomers according to any of claims 8-21, wherein the nucleic acid tags are configured to be concatenated to one another in solution upon reaching an interlocking spatial alignment.

23. A composition comprising a plurality of residue tagging monomers according to any of claims 8-22, wherein the nucleic-acid tag in the residue labelling moiety is a first oligonucleotide, whereby the second residue labelling moiety is a second oligonucleotide, and whereby the first oligonucleotide and the second oligonucleotide support extension of a nucleic acid sequence when two or more of the plurality of residue tagging monomers in solution reach an interlocking spatial alignment.

24. A method of generating a protein-derived nucleic-acid readout from a peptide, polypeptide, or protein, the method comprising:providing a plurality of residue-tagging monomers according to any of claims 1-23; contacting the peptide, polypeptide, or protein under conditions that render at least a portion of residues accessible;allowing the residue-recognition moieties to bind to their respective residues; concatenating at least a portion of the nucleic-acid tags of bound monomers to form a concatenated nucleic-acid sequence via interlocking spatial alignment of two or more residue recognition moieties; anddetecting the concatenated nucleic-acid sequence.

25. The method of claim 24, wherein rendering residues accessible comprises one or more of denaturation, fragmentation, backbone locking, helix stabilization, detergent treatment, or combinations thereof.

26. The method of claim 24 or 25, wherein concatenation is mediated by an enzymatic ligase, a splint oligonucleotide, a chemical coupling reaction, or combinations thereof.

27. The method of any of claims 24-26, further comprising releasing the concatenated nucleic-acid sequence from the monomers by denaturation, linker cleavage, nuclease digestion of a complementary strand, heat, ionic, or chemical treatment.

28. The method of any of claims 24-27, further comprising detecting, identifying, or quantifying a protein, protein isoform, protein modification, secondary or tertiary structure, orprotein-protein interaction using qPCR, digital PCR, next-generation sequencing, nanopore sequencing, Sanger sequencing, probe-based assays, or combinations thereof.

29. The method of any of claims 24-28, wherein the plurality comprises pre-linked residue-tagging monomers designed to target a predefined residue pattern.

30. The method of any of claims 24-29, further comprising adding a non-specific residue-tagging monomer to bind unoccupied residues before concatenation.

31. A method of characterizing a protein’s structural state comprising performing the method of any of claims 24-30 under non-denaturing conditions and deriving an interlocking planar orientation-dependent concatenated nucleic-acid readout indicative of secondary, tertiary, or quaternary structure.

32. A method of detecting a post-translational modification comprising performing the method of any of claims 24-31 using residue-tagging monomers specific for a modified residue and its corresponding unmodified residue and distinguishing the presence of the modification by sequence differences in the concatenated nucleic-acid readout.

33. The method of any of claims 24-32, wherein, after allowing a mixture of a plurality of residue recognition moieties to bind to their respective cognate residue of the amino acid or a residue of the polypeptide; an oligonucleotide that hybridizes to a residue-labeling moiety sequence associated with at least one bound residue-recognition moiety is added, and the bound residue of the amino acid or the residue of the polypeptide is detected by fluorescence readout or enriched by immunoprecipitation of the complex.

34. The method of claim 33, wherein the oligonucleotide is a splint oligonucleotide that hybridizes to a trans-residue-labeling moiety strand and comprises a capture or reporter moiety selected from biotin, digoxigenin, and a fluorophore.

35. The method of claim 34, wherein enrichment is performed by contacting the reaction mixture with a solid support which binds to a splint oligonucleotide or a trans- residuelabeling moiety strand hybridized thereto, followed by washing and elution of peptide-bound complexes.

36. The method of claim 35, wherein the solid support is streptavidin-coated magnetic beads to capture a biotinylated splint oligonucleotide or a biotinylated trans- residue-labeling moiety strand37. The method of any of claims 24-36, further comprising concatenating the residuelabeling moiety elements to generate a protein identifier DNA (pDNA) sequence corresponding to the sequence of amino acids contacted by the residue recognition moieties and quantifying the pDNA by quantitative PCR.

38. The method of claim 37, further comprising sequencing the pDNA by nanopore or Illumina next-generation sequencing to determine the order of residue-labeling moiety sequence elements and thereby resolve the polypeptide sequence recognized by the residue recognition moieties.

39. The method of any of claims 24-38, wherein the nucleic-acid tag in the residue labelling moiety is a first oligonucleotide, whereby the second residue labelling moiety is a second oligonucleotide, and whereby the first oligonucleotide and the second oligonucleotide support extension of a nucleic acid sequence when two or more of the plurality of residue tagging monomers in solution reach an interlocking spatial alignment.

40. The composition of any of the preceding composition claims, wherein the nucleic-acid tag length is 3-12 nucleotides and includes a 3’ one-base overhang.

41. The method of any of the preceding method claims, wherein concatenation uses SplintR ligase with a complementary splint oligonucleotide hybridizing to two adjacent tag strands.

42. A kit comprising:a plurality of residue-tagging monomers according to any of claims 1-23 targeting at least a subset of amino acid residues;at least one concatenation agent selected from an enzymatic ligase or a chemical coupling reagent; andinstructions for use.

43. The kit of claim 42, further comprising one or more of: a non-specific residue-tagging monomer; a set of pre-linked residue-tagging monomers; a splint oligonucleotide; sequencing adapters; and PCR primer sets.

44. The kit of claim 42 or 43, wherein the residue-tagging monomers are provided as single-stranded or double-stranded nucleic-acid tags with defined end chemistries to control concatenation orientation.

45. The kit of any of the preceding kit claims, wherein the linker is photocleavable and configured to release the concatenated readout on exposure to light.

46. The kit of any of the preceding claims, wherein the chemical coupling reagent is a nucleic acid extending enzyme, optionally wherein the nucleic acid extending enzyme is a DNA polymerase or an RNA polymerase.

Images