Analytical and Bioanalytical Chemistry

, Volume 397, Issue 3, pp 967–972 | Cite as

Hydrogen exchange mass spectrometry: what is it and what can it tell us?

Trends

Abstract

Proteins are undoubtedly some of the most essential molecules of life. While much is known about many proteins, some aspects still remain mysterious. One particularly important aspect of understanding proteins is determining how structure helps dictate function. Continued development and implementation of biophysical techniques that provide information about protein conformation and dynamics is essential. In this review, we discuss hydrogen exchange mass spectrometry and how this method can be used to learn about protein conformation and dynamics. The basic concepts of the method are described, the workflow illustrated, and a few examples of its application are provided.

Figure

Analysis of deuterium incorporation into protein with mass spectrometry

Keywords

Deuterium Protein mass spectrometry Protein dynamics Protein conformation 

Notes

Acknowledgements

We would like to thank Dr. Thomas Wales and Dr. Thomas Smithgall for the Lyn SH3:Nef binding data. This work was supported in part by the National Institutes of Health (R01-GM070590 and R01-GM086507). This is contribution 959 from the Barnett Institute.

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Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  1. 1.The Department of Chemistry & Chemical Biology and The Barnett Institute of Chemical & Biological AnalysisNortheastern UniversityBostonUSA
  2. 2.341 Mugar Life SciencesNortheastern UniversityBostonUSA

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