A complete understanding of enzyme catalysis requires knowledge of both transition state
features and the detailed motions of atoms that cause reactant molecules to form and …

This Perspective reviews the use of Transition Path Sampling methods to study
enzymatically catalyzed chemical reactions. First applied by our group to an enzymatic …

Using high-throughput microfluidic enzyme kinetics (HT-MEK), we measured over 9,000
inhibition curves detailing impacts of 1,004 single-site mutations throughout the alkaline …

Despite tremendous progress in understanding and engineering enzymes, knowledge of
how enzyme structures and their dynamics induce observed catalytic properties is …

The physical basis for enzymatic rate accelerations is a subject of great fundamental interest
and of direct relevance to areas that include the de novo design of green catalysts and the …

In recent years, there has been much discussion regarding the origin of enzymatic catalysis
and whether including protein dynamics is necessary for understanding catalytic …

Heavy enzyme isotope effects occur in proteins substituted with 2H-, 13C-, and 15N-
enriched amino acids. Mass alterations perturb femtosecond protein motions and have been …

Enzymes speed up biochemical reactions at the core of life by as much as 15 orders of
magnitude. Yet, despite considerable advances, the fine dynamical determinants at the …

β-Lactamases are one of the primary enzymes responsible for antibiotic resistance and have
existed for billions of years. The structural differences between a modern class A TEM-1 β …

Transition path-sampling calculations with several enzymes have indicated that local
catalytic site femtosecond motions are linked to transition state barrier crossing …