Enzymes continue to be the subject of intensive research efforts because of their ability to
accelerate chemical reactions by factors as large as 1020 with extraordinary selectivity. 1 …

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 …

Electrostatic interactions play an important role in enzyme catalysis by guiding ligand
binding and facilitating chemical reactions. These electrostatic interactions are modulated by …

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 …

This article illustrates by examples the limited acceptance by biologists of predictions made
with molecular dynamics simulations of biomolecules. Its purpose is to increase the …

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 …

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+ …

Theoretical and computational tools can provide a detailed knowledge of the mode of action
of enzymes. This knowledge can be systematized to be used as a guide for the design of …

Understanding the catalytic efficiency and specificity of enzymes is a fundamental question
of major practical and conceptual importance in biochemistry. Although progress in …

Ketosteroid isomerase (Δ5–3–keto steroid isomerase or steroid Δ–isomerase) is a highly
efficient enzyme at the centre of current debates on enzyme catalysis. We have modelled the …