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Protein Dynamics pp 3–27Cite as

Monitoring Side-Chain Dynamics of Proteins Using 2H Relaxation

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 1084))

Abstract

Nuclear magnetic resonance (NMR) is a powerful technique capable of monitoring a wide range of motions in proteins on a per residue basis. A variety of 2H relaxation experiments have been developed for monitoring side-chain methyl group motions on the picosecond–nanosecond timescale. These experiments enable determination of the order parameter, S 2 axis, which reports on the rigidity of the C-CH3 bond for side-chain methyl groups. The application of a commonly used subset of these experiments is described in this chapter. It is intended to serve as a practical guide to investigators interested in monitoring side-chain motions.

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Authors and Affiliations

  1. Division of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA

    Chad M. Petit & Andrew L. Lee

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  1. Chad M. Petit
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  2. Andrew L. Lee
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Editors and Affiliations

  1. Department of Bioinformatics and Genomic, University of North Carolina at Charlott, Charlotte, North Carolina, USA

    Dennis R. Livesay

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Petit, C.M., Lee, A.L. (2014). Monitoring Side-Chain Dynamics of Proteins Using 2H Relaxation. In: Livesay, D. (eds) Protein Dynamics. Methods in Molecular Biology, vol 1084. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-658-0_1

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  • DOI: https://doi.org/10.1007/978-1-62703-658-0_1

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  • Publisher Name: Humana Press, Totowa, NJ

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