title: Covariation of backbone motion throughout a small protein domain.
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.
authors.affiliation: Department of Chemistry, Indiana University, Bloomington, Indiana 47405-0001, USA.
authors.forename: Kristen L
authors.initials: KL
authors.lastname: Mayer
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Earley
authors.forename: Sonia
authors.initials: S
authors.lastname: Gupta
authors.forename: Kumar
authors.initials: K
authors.lastname: Pichumani
authors.forename: Lynne
authors.initials: L
authors.lastname: Regan
authors.forename: Martin J
authors.initials: MJ
authors.lastname: Stone
mesh_terms: D009154:Mutation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary