Covariation of backbone motion throughout a small protein domain

Kristen L. Mayer, Matthew R. Earley, Sonia Gupta, Kumar Pichumani, Lynne Regan, Martin J. Stone

Research output: Contribution to journalArticle

39 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)962-965
Number of pages4
JournalNature Structural Biology
Volume10
Issue number11
DOIs
StatePublished - Nov 1 2003

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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