NMR spectroscopy is a key method for studying the structure and dynamics of (large)
multidomain proteins and complexes in solution. It plays a unique role in integrated …

More than half of disease-causing missense variants are thought to lead to protein
degradation, but the molecular mechanism of how these variants are recognized by the cell …

Hydrogen atoms play a central role in many biochemical processes yet are difficult to
visualize by x-ray crystallography. Spallation neutron sources provide a new arena for …

The intracellular Ca2+ concentration is an important regulator of many cellular functions.
The small acidic protein calmodulin (CaM) serves as a Ca2+ sensor and control element for …

Conformational change is regulating the biological activity of a large number of proteins and
enzymes. Efforts in structural biology have provided molecular descriptions of the …

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 …

Numerous proteins require cofactors to be active. Computer simulations suggest that
cooperative interaction networks achieve optimal cofactor binding. There is a need for the …

To obtain insight into the motional features of proteins for enzymatic function, we studied
binding reactions between ferredoxin‐NADP+ reductase (FNR) and ferredoxin (Fd) using …

In order to examine the origins of the large positive cooperativity (Δ G 0coop=− 2.9 kcal mol−
1) of trimethoprim (TMP) binding to a bacterial dihydrofolate reductase (DHFR) in the …

Antimicrobial resistance presents a significant health care crisis. The mutation F98Y in
Staphylococcus aureus dihydrofolate reductase (SaDHFR) confers resistance to the …