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Conformational changes in proteins probed by hydrogen‐exchange electrospray‐ionization mass spectrometry
Author(s) -
Katta Viswanatham,
Chait Brian T.,
Carr Steven
Publication year - 1991
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290050415
Subject(s) - chemistry , electrospray ionization , mass spectrometry , protein mass spectrometry , extractive electrospray ionization , sample preparation in mass spectrometry , top down proteomics , chromatography , hydrogen–deuterium exchange , electrospray , analytical chemistry (journal)
Hydrogen‐exchange electrospray‐ionization mass spectrometry is demonstrated to be an effective new method for probing conformational changes of proteins in solutions. The method is based on the mass spectrometric measurement of the extent of hydrogen/deuterium exchange that occurs in different protein conformers over defined periods of time. Results are presented in which hydrogen‐exchange electrospray‐ionization mass spectrometry is used to probe conformational changes in bovine ubiquitin induced by the addition of methanol to aqueous acidic solutions of the protein.