Ontology highlight
ABSTRACT:
SUBMITTER: Jacobs WM
PROVIDER: S-EPMC5018131 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Jacobs William M WM Shakhnovich Eugene I EI
Biophysical journal 20160901 5
We propose a general theory to describe the distribution of protein-folding transition paths. We show that transition paths follow a predictable sequence of high-free-energy transient states that are separated by free-energy barriers. Each transient state corresponds to the assembly of one or more discrete, cooperative units, which are determined directly from the native structure. We show that the transition state on a folding pathway is reached when a small number of critical contacts are form ...[more]