Covariation of backbone motion throughout a small protein domain. Academic Article uri icon

Overview

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.

publication date

  • October 5, 2003

Research

keywords

  • Protein Conformation
  • Protein Structure, Tertiary

Identity

Scopus Document Identifier

  • 0242490496

PubMed ID

  • 14528292

Additional Document Info

volume

  • 10

issue

  • 11