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Measurement of Intermediate Exchange Phenomena

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Protein NMR Techniques

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 278))

Abstract

Understanding the crucial role of protein motions in the function of biological macromolecules requires methods for their characterization. These motions lead to noticeable alterations in the decay of nuclear spin magnetization. Recent advances in solution nuclear magnetic resonance (NMR) make quantitative connections between µs–ms motions and nuclear spin relaxation in proteins. The techniques serve as useful probes of motional kinetics and thermodynamics and their relation to function. Here, we review the two most common experimental methods for characterizing conformational motions in proteins: the relaxation-compensated Carr-Purcell-Meiboom-Gill (rcCPMG) and off-resonance experiments.

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

    James G. Kempf & J. Patrick Loria

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  1. James G. Kempf
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  1. Department of Biochemistry, University of Oxford, Oxford, UK

    A. Kristina Downing

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Kempf, J.G., Loria, J.P. (2004). Measurement of Intermediate Exchange Phenomena. In: Downing, A.K. (eds) Protein NMR Techniques. Methods in Molecular Biology™, vol 278. Humana Press. https://doi.org/10.1385/1-59259-809-9:185

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  • DOI: https://doi.org/10.1385/1-59259-809-9:185

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-246-9

  • Online ISBN: 978-1-59259-809-0

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