Abstract
Hydrogen/deuterium exchange electrospray ionization mass spectrometry is demonstrated to be effective in probing changes in the conformation of proteins in solution. 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 the method is used to probe conformational changes in (a) bovine ubiquitin induced by the addition of methanol to aqueous acidic solutions and (b) chicken egg lysozyme caused by the reduction of the intramolecular disulfide cross-linkages.
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