Ontology highlight
ABSTRACT:
SUBMITTER: Loveridge EJ
PROVIDER: S-EPMC3590880 | biostudies-literature | 2011 Dec
REPOSITORIES: biostudies-literature
Loveridge E Joel EJ Tey Lai-Hock LH Behiry Enas M EM Dawson William M WM Evans Rhiannon M RM Whittaker Sara B-M SB Günther Ulrich L UL Williams Christopher C Crump Matthew P MP Allemann Rudolf K RK
Journal of the American Chemical Society 20111122 50
Dihydrofolate reductase has long been used as a model system to study the coupling of protein motions to enzymatic hydride transfer. By studying environmental effects on hydride transfer in dihydrofolate reductase (DHFR) from the cold-adapted bacterium Moritella profunda (MpDHFR) and comparing the flexibility of this enzyme to that of DHFR from Escherichia coli (EcDHFR), we demonstrate that factors that affect large-scale (i.e., long-range, but not necessarily large amplitude) protein motions ha ...[more]