Ontology highlight
ABSTRACT:
SUBMITTER: Dong M
PROVIDER: S-EPMC7021514 | biostudies-literature | 2020 Jan
REPOSITORIES: biostudies-literature
Dong Ming M Lauro Mackenzie L ML Koblish Timothy J TJ Bahnson Brian J BJ
Structural dynamics (Melville, N.Y.) 20200101 1
Numerous studies have suggested a significant role that protein dynamics play in optimizing enzyme catalysis, and changes in conformational sampling offer a window to explore this role. Thermolysin from <i>Bacillus thermoproteolyticus rokko</i>, which is a heat-stable zinc metalloproteinase, serves here as a model system to study changes of protein function and conformational sampling across a temperature range of 16-36 °C. The temperature dependence of kinetics of thermolysin showed a biphasic ...[more]