Ontology highlight
ABSTRACT:
SUBMITTER: Andrews BT
PROVIDER: S-EPMC3601837 | biostudies-literature | 2013 Jan
REPOSITORIES: biostudies-literature
Andrews Benjamin T BT Capraro Dominique T DT Sulkowska Joanna I JI Onuchic José N JN Jennings Patricia A PA
The journal of physical chemistry letters 20121218 1
Topologically complex proteins fold by multiple routes as a result of hard-to-fold regions of the proteins. Oftentimes these regions are introduced into the protein scaffold for function and increase frustration in the otherwise smooth-funneled landscape. Interestingly, while functional regions add complexity to folding landscapes, they may also contribute to a unique behavior referred to as hysteresis. While hysteresis is predicted to be rare, it is observed in various proteins, including prote ...[more]