Conformational analysis of processivity clamps in solution demonstrates that tertiary structure does not correlate with protein dynamics.

ABSTRACT: The relationship between protein sequence, structure, and dynamics has been elusive. Here, we report a comprehensive analysis using an in-solution experimental approach to study how the conservation of tertiary structure correlates with protein dynamics. Hydrogen exchange measurements of eight processivity clamp proteins from different species revealed that, despite highly similar three-dimensional structures, clamp proteins display a wide range of dynamic behavior. Differences were apparent both for structurally similar domains within proteins and for corresponding domains of different proteins. Several of the clamps contained regions that underwent local unfolding with different half-lives. We also observed a conserved pattern of alternating dynamics of the α helices lining the inner por

SUBMITTER: Fang J 

PROVIDER: S-EPMC3984358 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature