Since its inception nearly a half century ago, CHARMM has been playing a central role in
computational biochemistry and biophysics. Commensurate with the developments in …

Conspectus The role of the enzyme's dynamic motions in catalysis is at the center of heated
contemporary debates among both theoreticians and experimentalists. Resolving these …

Substrate positioning dynamics (SPD) orients the substrate in the active site, thereby
influencing catalytic efficiency. However, it remains unknown whether SPD effects originate …

Enzymes undergo a range of internal motions from local, active site fluctuations to large‐
scale, global conformational changes. These motions are often important for enzyme …

Residues beyond the first coordination shell are often observed to make considerable
cumulative contributions in enzymes. Due to typically indirect perturbations of multiple …

The role of protein motions in promoting the chemical step of enzyme catalysed reactions
remains a subject of considerable debate. Here, a unified view of the role of protein …

Molecular dynamics calculations and bionformatic studies of dihydrofolate reductase
(DHFR) have suggested a network of coupled motions across the whole protein that is …

Chemical ligation has been used to alter motions in specific regions of dihydrofolate
reductase from E. coli and to investigate the effects of localized motional changes on …

Escherichia coli dihydrofolate reductase (ecDHFR) is used to study fundamental principles
of enzyme catalysis. It remains controversial whether fast protein motions are coupled to the …

A high-pressure crystallographic study was conducted on Escherichia coli dihydrofolate
reductase (ecDHFR) complexed with folate and NADP+ in crystal forms containing both the …