Conspectus Because living organisms are in constant motion, the word “dynamics” can hold
many meanings to biologists. Here we focus specifically on the conformational changes that …

Solving structures or structural ensembles of large macromolecular systems in solution
poses a challenging problem. While NMR provides structural information at atomic …

Detailed descriptions of atomic coordinates and motions are required for an understanding
of protein dynamics and their relation to molecular recognition, catalytic function, and …

The traditional structure–function paradigm has provided significant insights for well-folded
proteins in which structures can be easily and rapidly revealed by X-ray crystallography …

We report the effect of conformational dynamics on the fluctuations of electric fields in the
active site of the enzyme ketosteroid isomerase (KSI). While KSI is considered to be a rigid …

Enzymes employ a wide range of protein motions to achieve efficient catalysis of chemical
reactions. While the role of collective protein motions in substrate binding, product release …

The successful simulation of proteins by molecular dynamics (MD) critically depends on the
accuracy of the applied force field. Here, we modify the AMBER-family ff99SBnmr2 force …

Side chain entropy and mutual entropy information between residue pairs have been
calculated for two de novo designed Kemp eliminase enzymes, KE07 and KE70, and for …

The rate-determining step in the catalytic cycle of E. coli dihydrofolate reductase is
tetrahydrofolate (THF) product release, which can occur via an allosteric or an intrinsic …

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