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Hydrogen Exchange Mass Spectrometry for Conformational Analysis of Proteins

Peptides and Proteins

  1. John R. Engen,
  2. Thomas E. Wales,
  3. Xiaomeng Shi

Published Online: 15 SEP 2011

DOI: 10.1002/9780470027318.a9201

Encyclopedia of Analytical Chemistry

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. .

Author Information

  1. Northeastern University, Department of Chemistry & Chemical Biology and the Barnett Institute of Chemical and Biological Analysis, Boston, MA, USA

Publication History

  1. Published Online: 15 SEP 2011

Abstract

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.