52 results about "Protein primary structure" patented technology

The cobra neurotoxin is capable of binding to nicotinic acetylcholine receptors after nerve synapses to block neuronal caudal ion flow to realize analgesic effect, however, the product on the market takes 2 hours to be effective and the curative effect is unstable, which cannot meet clinical requirement. The neurotoxins need to pass a blood cerebral barrier in the brain to play an analgesic effect, and the product on the market has no clear components, including various molecular weight proteins, so the speed for permeating the blood cerebral barrier is slow; and at the same time, affinity with the nicotinic acetylcholine receptors is also inconsistent. The application screens a group of neurotoxin molecular monomers having high affinity with the nicotinic acetylcholine receptor, can quickly pass the blood cerebral barrier, and has analgesic effect and stable therapeutic effect in 30 minutes. The neurotoxin molecular monomer overcomes the defects that a mixture cannot specify which neurotoxin is present, the protein primary structure is not existed, the quality cannot be precisely controlled; according to the invention, the quality is controlled, clinical safety and effectiveness are better guaranteed.

A protein structure capable of selective interaction with an organic target is provided. The protein structure is a polymer comprising as a repeating structural unit a recombinant fusion protein that is capable of selective interaction with the organic target. The fusion protein is comprising the moieties B, REP and CT, and optionally NT. B is a non-spidroin moiety of more than 30 amino acid residues, which provides the capacity of selective interaction with the organic target. REP is a moiety of from 70 to 300 amino acid residues and is derived from the repetitive fragment of a spider silk protein. CT is a moiety of from 70 to 120 amino acid residues and is derived from the C-terminal fragment of a spider silk protein. NT is an optional moiety of from 100 to 160 amino acid residues and is derived from the N-terminal fragment of a spider silk protein. The fusion protein and protein structure thereof is useful as an affinity medium and a cell scaffold material.

The present invention relates to a method for predicting three-dimensional structure of a protein from its sequence. Three-dimensional structure may be determined by: (a) generating a multiple sequence alignment for a candidate protein having a known sequence; (b) identifying a covariance matrix between all pairs of sequence positions in the multiple sequence alignment; (c) inverting the covariance matrix and identifying predicted evolutionary constraints using a statistical model of the candidate protein; and (d) simulating folding of an extended chain structure of the candidate protein using the predicted constraints.

The present invention provides methods for stabilizing a biological sample for analysis. The invention more particularly provides methods combining heat treatment and chemical fixation of biological samples in order to maintain protein primary structure and post-translational modifications, such as protein phosphorylations.

It is intended to provide a method of analyzing a change in the primary structure of a nucleic acid which is excellent in quantification properties, achieves a high sensitivity and a high reproducibility and can be quickly conducted at a low cost. Namely, a method of analyzing a change in the primary structure of a nucleic acid characterized by comprising: the step of obtaining nucleic acids wherein a first ligand and a second ligand differing from each other in nucleic acid type are bound to the standard sequence in a standard nucleic acid and a target sequence in a subject nucleic acid to be analyzed; the step of specifically binding the first ligand to a receptor held on a support to thereby immobilize the standard sequence and the target sequence to the support; the step of specifically binding a labeled receptor to the second ligand in the nucleic acids thus immobilized; the step of detecting the label to thereby detect the standard sequence and the target sequence; the step of determining the ratio of the standard sequence in the standard nucleic acid and the target nucleic acid to be analyzed, thus calculating a coefficient for correcting the detection data of the target sequence followed by the correction; and the step of confirming an increase or a decrease in the amount of the target sequence in the subject nucleic acid to be analyzed compared with the target sequence in the standard nucleic acid.

Described herein are rules to modify natural mRNAs or to engineer synthetic mRNAs to increase their translation efficiencies. These rules describe modifications to mRNA coding and 3' UTR sequences intended to enhance protein synthesis by: 1) decreasing ribosomal diversion via AUG or non-canonical initiation codons in coding sequences, and / or 2) by evading miRNA-mediated down-regulation by eliminating one or more miRNA binding sites in coding sequences.