Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering.

ABSTRACT: One of the most challenging tasks in biological science is to understand how a protein folds. In theoretical studies, the hypothesis adopting a funnel-like free-energy landscape has been recognized as a prominent scheme for explaining protein folding in views of both internal energy and conformational heterogeneity of a protein. Despite numerous experimental efforts, however, comprehensively studying protein folding with respect to its global conformational changes in conjunction with the heterogeneity has been elusive. Here we investigate the redox-coupled folding dynamics of equine heart cytochrome c (cyt-c) induced by external electron injection by using time-resolved X-ray solution scattering. A systematic kinetic analysis unveils a kinetic model for its folding with a stretched

SUBMITTER: Kim TW 

PROVIDER: S-EPMC7334511 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature