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Dynamic activation of protein function: A view emerging from NMR spectroscopy

Nature Structural Biology volume 8, pages 926–931 (2001)Cite this article

Abstract

Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion to report on the residual conformational entropy of proteins and how this entropy can enter into both the thermodynamic and kinetic aspects of protein function.

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Figure 1: Illustration of various motions affecting the obtained generalized order parameters for methyl deuterons.
Figure 2: Distributions of the amplitude of fast dynamics of methyl-bearing side chains in proteins.
Figure 3: Fast dynamics of methyl-bearing side chains in a calmodulin-peptide complex.
Figure 4: Dynamics, entropy and allostery.

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Acknowledgements

I thank A. Palmer, K. Sharp and W. Englander for helpful discussion. This work was supported by grants from the NIH.

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  1. The Johnson Research Foundation & Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, 19104, Pennsylvania, USA

    A. Joshua Wand

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Wand, A. Dynamic activation of protein function: A view emerging from NMR spectroscopy. Nat Struct Mol Biol 8, 926–931 (2001). https://doi.org/10.1038/nsb1101-926

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