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Protein dynamics from NMR

Nature Structural Biology volume 7, pages 740–743 (2000)Cite this article

Abstract

This review surveys recent investigations of conformational fluctuations of proteins in solution using NMR techniques. Advances in experimental methods have provided more accurate means of characterizing fast and slow internal motions as well as overall diffusion. The information obtained from NMR dynamics experiments provides insights into specific structural changes or configurational energetics associated with function. A variety of applications illustrate that studies of protein dynamics provide insights into protein–protein interactions, target recognition, ligand binding, and enzyme function.

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Figure 1: Relationship between internal motion and model-free parameters.

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Authors and Affiliations

  1. Molecular Structural Biology Unit, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, 20892, Maryland, USA

    Rieko Ishima & Dennis A. Torchia

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  1. Rieko Ishima
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  2. Dennis A. Torchia
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Correspondence to Rieko Ishima or Dennis A. Torchia.

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Ishima, R., Torchia, D. Protein dynamics from NMR. Nat Struct Mol Biol 7, 740–743 (2000). https://doi.org/10.1038/78963

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