Hydrogen Exchange Mass Spectrometry for Conformational Analysis of Proteins
Peptides and Proteins
Published Online: 15 SEP 2011
Copyright © 2000 John Wiley & Sons, Ltd. All rights reserved.
Encyclopedia of Analytical Chemistry
How to Cite
Engen, J. R., Wales, T. E. and Shi, X. 2011. Hydrogen Exchange Mass Spectrometry for Conformational Analysis of Proteins. Encyclopedia of Analytical Chemistry. .
- Published Online: 15 SEP 2011
Proteins contain labile hydrogen atoms at the backbone amide positions. These hydrogens are in continuous exchange with hydrogen in surrounding solvent. By incubating proteins with an isotope of hydrogen, usually deuterium, this exchange process can be monitored experimentally. Because hydrogen exchange (HX) is a function of protein conformation and dynamics, the rate of HX reports on aspects of protein structure. One method for detection of exchange is mass spectrometry (MS), as proteins will increase in mass as deuteration proceeds. This article provides background on how and why hydrogens exchange, how the exchange is controlled by several parameters, and what measuring exchange is good for, and then gives a general overview of how to make these measurements with MS.