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Covariation of backbone motion throughout a small protein domain

Nature Structural & Molecular Biology volume 10, pages 962–965 (2003)Cite this article

Abstract

The synchronization (correlation) of conformational fluctuations in folded proteins may influence the rates of enzyme catalysis and ligand binding as well as the stabilities of native proteins and their complexes. However, experimental detection of correlated motions remains difficult. Herein, we present an analysis of the covariation of NMR-derived backbone dynamical parameters among a family of ten mutants of a small protein. Both the spatial restriction and the time scales of backbone motions exhibit a higher degree of covariation than would be expected if the internal motions of each group were independent, providing experimental support for correlated dynamics. Application of this approach to other proteins may reveal dynamical correlations that influence catalysis, ligand-binding and/or protein stability.

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Figure 1: Ribbon representation of the B1 domain of protein G.
Figure 2: Covariation of dynamics parameters for the B1 domain.
Figure 3: Structural distribution of dynamical covariations.

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Acknowledgements

We thank J.L. Vaughn for discussions. This work was supported by grants from the US National Science Foundation and the American Chemical Society Petroleum Research Fund.

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Authors and Affiliations

  1. Department of Chemistry, Indiana University, Bloomington, 47405-0001, Indiana, USA

    Kristen L Mayer, Matthew R Earley, Sonia Gupta, Kumar Pichumani & Martin J Stone

  2. Department of Chemistry and Department of Molecular Biophysics and Biochemistry, Yale University, PO Box 208114, 266 Whitney Avenue, New Haven, 06520-8114, Connecticut, USA

    Lynne Regan

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Correspondence to Martin J Stone.

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Mayer, K., Earley, M., Gupta, S. et al. Covariation of backbone motion throughout a small protein domain. Nat Struct Mol Biol 10, 962–965 (2003). https://doi.org/10.1038/nsb991

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