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Investigating the Higher Order Structure of Proteins

Hydrogen Exchange, Proteolytic Fragmentation, and Mass Spectrometry

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Mass Spectrometry of Proteins and Peptides

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 146))

Abstract

It has been apparent for some years that the structures of proteins are dynamic rather than static. For some proteins, dynamics is essential to function (e.g., refs. 1–7). These structural changes have been detected for more than 30 yr by observing hydrogen exchange between peptide amide hydrogens and solvent containing the hydrogen isotopes tritium or deuterium (8–10). Although tritium is no longer used extensively for this purpose, deuterium is widely used in hydrogen exchange studies, especially in multidimensional nuclear magnetic resonance (NMR), in which amide hydrogen signals disappear on deuteration. Since deuterium weighs 1 Dalton more than protium, hydrogen exchange in proteins can also be detected by mass spectrometry. This approach is complementary to NMR in some respects and clearly advantageous in others.

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Author information

Authors and Affiliations

  1. Department of Chemistry, University of Nebraska-Lincoln, Lincoln, NE

    John R. Engen

  2. Department of Chemistry, University of Nebraska-Lincoln, Lincoln, NE

    David L. Smith

Authors
  1. John R. Engen
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  2. David L. Smith
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Editors and Affiliations

  1. Sale, Manchester, UK

    John R. Chapman

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© 2000 Humana Press Inc.

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Engen, J.R., Smith, D.L. (2000). Investigating the Higher Order Structure of Proteins. In: Chapman, J.R. (eds) Mass Spectrometry of Proteins and Peptides. Methods in Molecular Biology™, vol 146. Humana Press, Totowa, NJ. https://doi.org/10.1385/1-59259-045-4:95

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  • DOI: https://doi.org/10.1385/1-59259-045-4:95

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-0-89603-609-3

  • Online ISBN: 978-1-59259-045-2

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