All soluble proteins populate conformational ensembles that together constitute the native
state. Their fluctuations in water are intrinsic thermodynamic phenomena, and the …

The relationship between protein dynamics and function is a subject of considerable
contemporary interest. Although protein motions are frequently observed during ligand …

Fast motions (femtosecond to picosecond) and their potential involvement during enzyme-
catalysed reactions have ignited considerable interest in recent years. Their influence on …

This Perspective presents a review of our work and that of others in the highly controversial
topic of the coupling of protein dynamics to reaction in enzymes. We have been involved in …

Despite the fact that the number of publications associated with the keyword'enzyme'
increases every year, the precise origin of enzyme catalysis has remained unresolved …

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

Experimental analysis of enzymatic transition-state structures uses kinetic isotope effects
(KIEs) to report on bonding and geometry differences between reactants and the transition …

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

Enzymes achieve their transition states by dynamic conformational searches on the
femtosecond to picosecond time scale. Mimics of reactants at enzymatic transition states …

We use quantized molecular dynamics simulations to characterize the role of enzyme
vibrations in facilitating dihydrofolate reductase hydride transfer. By sampling the full …