Direct observation of parallel folding pathways revealed using a symmetric repeat protein system.

ABSTRACT: Although progress has been made to determine the native fold of a polypeptide from its primary structure, the diversity of pathways that connect the unfolded and folded states has not been adequately explored. Theoretical and computational studies predict that proteins fold through parallel pathways on funneled energy landscapes, although experimental detection of pathway diversity has been challenging. Here, we exploit the high translational symmetry and the direct length variation afforded by linear repeat proteins to directly detect folding through parallel pathways. By comparing folding rates of consensus ankyrin repeat proteins (CARPs), we find a clear increase in folding rates with increasing size and repeat number, although the size of the transition states (estimated from denaturan

SUBMITTER: Aksel T 

PROVIDER: S-EPMC4119276 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature