Ontology highlight
ABSTRACT:
SUBMITTER: Vaughn MB
PROVIDER: S-EPMC5802873 | biostudies-literature | 2018 Jan
REPOSITORIES: biostudies-literature
Vaughn Morgan B MB Zhang Jianyu J Spiro Thomas G TG Dyer R Brian RB Klinman Judith P JP
Journal of the American Chemical Society 20180111 3
Previous studies of a thermophilic alcohol dehydrogenase (ht-ADH) demonstrated a range of discontinuous transitions at 30 °C that include catalysis, kinetic isotope effects, protein hydrogen-deuterium exchange rates, and intrinsic fluorescence properties. Using the Förster resonance energy transfer response from a Trp-NADH donor-acceptor pair in T-jump studies of ht-ADH, we now report microsecond protein motions that can be directly related to active site chemistry. Two distinctive transients ar ...[more]