How well does a funneled energy landscape capture the folding mechanism of spectrin domains?

ABSTRACT: Three structurally similar domains from α-spectrin have been shown to fold very differently. First, there is a contrast in the folding mechanism, as probed by Φ-value analysis, between the R15 domain and the R16 and R17 domains. Second, there are very different contributions from internal friction to folding: the folding rate of the R15 domain was found to be inversely proportional to solvent viscosity, showing no apparent frictional contribution from the protein, but in the other two domains, a large internal friction component was evident. Non-native misdocking of helices has been suggested to be responsible for this phenomenon. Here, I study the folding of these three proteins with minimalist coarse-grained models based on a funneled energy landscape. Remarkably, I find that, despite th

SUBMITTER: Best RB 

PROVIDER: S-EPMC3808457 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature