86 results about "Maldi ms" patented technology

A simple and efficient method of preparing a sample in the measurement according to matrix-assisted laser desorption / ionization mass spectrometry (MALDI-MS) capable of inhibiting any ion suppression by impurities, such as inorganic salts and surfactants, contained in the sample. An analyte and matrix molecules are co-crystallized in the presence of porous microparticles. Preferably, this co-crystallization is carried out by bringing the analyte, matrix molecules and porous microparticles into contact with each other on a target plate and thereafter drying the mixture. The porous microparticles consist of an ion exchanger having an average particle diameter of not more than 50 μm, preferably a strongly basic anion exchanger.

A MALDI plate suitable for MS or MS-MS analysis provided with a composite coating that comprises a hydrophobic coating and a thin layer coating of a mixture of a MALDI matrix material and an intercalating agent such as a polymer is disclosed. A MALDI plate produced in accordance with the present teachings is useful for suppression of matrix ions in the low mass region (<1,000 daltons) of a MALDI-MS spectrum.

This invention provides a device and methods for increasing the concentration of a charged species in solution, wherein the solution containing the concentrated species is exposed to the environment. Such solution can be formed on a surface or on a tip of a measurement device. The open-environment concentration technique overcomes the disadvantages of in-channel concentration devices, especially by eliminating flow-induced delivery processes that lead to concentration losses. Combined with direct contact dispensing, methods of this invention can be used for various applications such as immunoassay and MALDI-MS.

Cleavable compositions and methods of use especially in MALDI MS analysis of hydrophobic proteins.

Embodiments of a method for demonstrating type and / or source of hair damage comprises extracting protein fragments from a hair sample with an aqueous solution, testing the resulting protein fragments with the MALDI-MS test, and then either comparing the results between a damaged sample and an undamaged sample or comparing the results between a damaged sample and a list of known marker protein fragments to identify the type and / or source of the damage.

In proteomic research, it is often necessary to screen a large number of polypeptides for the presence of stable structure. Described herein are methods (referred to as MALDI MS-HX and SUPREX) for measuring the stability of proteins in a rapid, high-throughput fashion. The method employs hydrogen exchange to estimate the stability of quantities of unpurified protein extracts, using matrix-assisted laser desorption / ionization (MALDI) mass spectrometry. A method of quantitatively determining the stability of a test protein under native conditions is disclosed. The method includes the steps (a) providing a test protein; (b) contacting the protein with an exchange buffer comprising a denaturant and deuterium, the exchange buffer having a denaturant concentration; (c) contacting the test protein with a mass spectrometry matrix medium; (d) determining a change in mass of the test protein by mass spectrometry; (e) varying the denaturant concentration of the exchange buffer; (f) repeating steps (a)-(e) a desired number of times; and (g) quantitatively determining protein stability based on the change in mass of the test protein as a function of denaturant concentration, whereby the stability of a test protein under native conditions is quantitatively determined.