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Hydrogen Exchange Techniques

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Protein Stability and Folding

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 40))

Abstract

Hydrogen exchange, in conjunction with NMR spectroscopy, is the only method with which one can, in principle, monitor protein folding and stability at nearly every individual amino acid residue in a protein. The unique power of hydrogen exchange is attributable to the ubiquity and the chemistry of the peptide NH group in proteins: Peptide NHs are labile to exchange with hydrogens of the aqueous solvent, and exchange often is slowed by many orders of magnitude in native proteins. If the hydrogen isotope in water is deuterium, then the exchange event in a vast excess of D2O can be summarized in the following scheme:

Deuterons are silent in a proton NMR experiment, so the resonances corresponding to the peptide NH will diminish in intensity as exchange proceeds. If NH resonance assignments have been made for the peptide or protein of interest, then exchange can be monitored at known sites throughout the sequence and structure.

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Author information

Authors and Affiliations

  1. Department of Medical Biochemistry and Genetics, Texas A & M University, College Station, TX

    J. Martin Scholtz

  2. Department of Biochemistry, University of Iowa, Iowa City, IA

    Andrew D. Robertson

Authors
  1. J. Martin Scholtz
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  2. Andrew D. Robertson
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Editor information

Editors and Affiliations

  1. Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, CT

    Bret A. Shirley

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© 1995 Humana Press Inc.

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Scholtz, J.M., Robertson, A.D. (1995). Hydrogen Exchange Techniques. In: Shirley, B.A. (eds) Protein Stability and Folding. Methods in Molecular Biology™, vol 40. Humana Press. https://doi.org/10.1385/0-89603-301-5:291

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  • DOI: https://doi.org/10.1385/0-89603-301-5:291

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-301-6

  • Online ISBN: 978-1-59259-527-3

  • eBook Packages: Springer Protocols

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