Ontology highlight
ABSTRACT:
SUBMITTER: Craig PO
PROVIDER: S-EPMC3203634 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20111006 43
Simulations based on perfectly funneled energy landscapes often capture many of the kinetic features of protein folding. We examined whether simulations based on funneled energy functions can also describe fluctuations in native-state protein ensembles. We quantitatively compared the site-specific local stability determined from structure-based folding simulations, with hydrogen exchange protection factors measured experimentally for ubiquitin, chymotrypsin inhibitor 2, and staphylococcal nuclea ...[more]