Article
Hairpin folding rates reflect mutations within and remote from the turn region.
Proceedings of the National Academy of Sciences of the United States of America - 25 Oct 2005
Olsen Katherine A, Fesinmeyer R Matthew, Stewart James M, Andersen Niels H
Abstract excerpt
Hairpins play a central role in numerous protein folding and misfolding scenarios. Prior studies of hairpin folding, many conducted with analogs of a sequence from the B1 domain of protein G, suggest that faster folding can be achieved only by optimizing the turn propensity of the reversing loop. Based on studies using dynamic NMR, the native GB1 sequence is a slow folding hairpin (k(F)(278)=1.5 x 10(4)/s). GB1...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
