Computational enzymology is a rapidly maturing field that is increasingly integral to
understanding mechanisms of enzyme-catalyzed reactions and their practical applications …

The growing momentum of several common life-style diseases such as myocardial
infarction, cardiovascular disorders, stroke, hypertension, diabetes, and atherosclerosis has …

What are the atomic motions at enzymatic catalytic sites on the timescale of chemical
change? Combined experimental and computational chemistry approaches take advantage …

Recent data increasingly reveal that conformational dynamics are indispensable to enzyme
function throughout the catalytic cycle, in substrate recruiting, chemical transformation, and …

Quasi-classical molecular dynamics (MD) simulations were carried out to study the
mechanism of iron porphyrin-catalyzed hydroxylation of ethylbenzene. The hydrogen atom …

Protein dynamics have controversially been proposed to be at the heart of enzyme catalysis,
but identification and analysis of dynamical effects in enzyme-catalyzed reactions have …

This article is an essay that discusses the concepts underlying the application of modern
transition state theory to reactions in enzymes. Issues covered include the potential of mean …

The role of protein dynamics in enzyme catalysis is one of the most active and controversial
areas in enzymology today. Some researchers claim that protein dynamics are at the heart …

The potential for femtosecond to picosecond time-scale motions to influence the rate of the
intrinsic chemical step in enzyme-catalyzed reactions is a source of significant controversy …

In recent years, the temperature dependence of primary kinetic isotope effects (KIE) has
been used as indicator for the physical nature of enzyme-catalyzed H-transfer reactions. An …