The purpose of this review is to demonstrate the critical importance of understanding protein–
excipient interactions as a key step in the rational design of formulations to stabilize and …

NMR spectroscopy is a powerful tool for studying the structure, function and dynamics of
biological macromolecules. However, non‐spectroscopists often find NMR theory daunting …

Protein dynamics on the atomic level and on the microsecond timescale has recently
become accessible from both computation and experiment. To validate molecular dynamics …

Despite their importance for biological activity, slower molecular motions beyond the
nanosecond range remain poorly understood. We have assembled an unprecedented set of …

Objective The coronavirus disease 2019 (COVID-19) pandemic has caused an exponential
rise in death rates and hospitalizations. The aim of this study was to characterize the D614G …

Relationships between protein structure and ionization of carboxyl groups were investigated
in 24 proteins of known structure and for which 115 aspartate and 97 glutamate pKa values …

Despite their crucial role in the stabilization of biomolecular structures and their almost
ubiquitous involvement in biomolecular reactions, such as enzymatic cleavage or ligand …

Recent trends in theoretical calculations of indirect spin–spin coupling constants covering
the period of May 2003–July 2006 are outlined with the emphasis on the currently used …

Hydrogen bonds profoundly influence the architecture and activity of biological
macromolecules. Deep appreciation of hydrogen bond contributions to biomolecular …

The temperature-dependence of a large number of NMR parameters describing hydrogen
bond properties in the protein ubiquitin was followed over a range from 5 to 65° C. The …