Recent years have seen an explosion in computer power, allowing for the examination of
ever more challenging problems. For instance, a recent simulation study, which was the first …

This brief review analyzes the underlying physical principles of enzyme catalysis, with an
emphasis on the role of equilibrium enzyme motions and conformational sampling. The …

Enzymes use protein architectures to create highly specialized structural motifs that can
greatly enhance the rates of complex chemical transformations. Here, we use experiments …

Understanding the electrostatic forces and features within highly heterogeneous,
anisotropic, and chemically complex enzyme active sites and their connection to biological …

In this review we give an overview of the field of Computational enzymology. We start by
describing the birth of the field, with emphasis on the work of the 2013 chemistry Nobel …

The vibrational Stark effect provides insight into the roles of hydrogen bonding,
electrostatics, and conformational motions in enzyme catalysis. In a recent application of this …

Hydrogen-bond networks play vital roles in biological functions ranging from protein folding
to enzyme catalysis. Here we combine electronic structure calculations and ab initio path …

The periplasmic Cu+/Ag+ chaperone CusF features a novel cation− π interaction between a
Cu+/Ag+ ion and Trp44 at the metal binding site. The nature and strength of the Cu+/Ag+ …

It is well-known that single H3N− HCl and H2O− HCl acid− base pairs do not react to form
the ion pairs, H4N+ Cl− and H3O+ Cl−, in isolation. On the basis of ab initio method, we …

Understanding how electric fields and their fluctuations in the active site of enzymes affect
efficient catalysis represents a critical objective of biochemical research. We have directly …