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Monitoring Molecular Interactions by NMR

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Protein Structure, Stability, and Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 490))

Abstract

The ability of proteins to interact with small molecules or other proteins is essential in all aspects of biology. In many cases these interactions cause detectable changes in NMR chemical shifts, lineshapes, and relaxation rates and therefore provide a means by which to study these biologically important phenomena. Here we review the theory upon which this analysis is based, provide several illustrative examples, and highlight potential problems in the study of binding interactions by solution NMR.

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Acknowledgements

JPL acknowledges support from the National Institutes of Health (R01-GM070823) and National Science Foundation (MCB0236966). JML is supported by an NIH biophysical training grant (GM08283).

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  1. Department of Chemistry, Yale University, New Haven, CT, USA

    James M. Lipchock & J. Patrick Loria

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  1. James M. Lipchock
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  2. J. Patrick Loria
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    © 2009 Humana Press, a part of Springer Science+Business Media, LLC

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    Lipchock, J.M., Loria, J.P. (2009). Monitoring Molecular Interactions by NMR. In: Shriver, J. (eds) Protein Structure, Stability, and Interactions. Methods in Molecular Biology, vol 490. Humana Press. https://doi.org/10.1007/978-1-59745-367-7_5

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    • DOI: https://doi.org/10.1007/978-1-59745-367-7_5

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    • Publisher Name: Humana Press

    • Print ISBN: 978-1-58829-954-3

    • Online ISBN: 978-1-59745-367-7

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