Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.

ABSTRACT: Small single domain proteins that fold on the microsecond time scale have been the subject of intense interest as models for probing the complexity of folding energy landscapes. The villin headpiece subdomain (HP36) has been extensively studied because of its simple three helix structure, ultrafast folding lifetime of a few microseconds, and stable native fold. We have previously shown that folding as measured by a single ¹³C═¹⁸O isotopic label on residue A57 in helix 2 occurs at a different rate than that measured by global probes of folding, indicating noncooperative complexity in the folding of HP36. In order to determine whether this complexity reflects intermediates or parallel pathways over a small activation barrier, ¹³C═¹⁸O labels were in

SUBMITTER: Nagarajan S 

PROVIDER: S-EPMC6395539 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature