Enzyme catalysis is an inherently dynamic process. Binding and release of ligands is often
accompanied by conformational changes, both subtle and dramatic (reviewed more …

▪ Abstract We describe large scale ab initio quantum chemical and mixed quantum
mechanics/molecular mechanics (QM/MM) methods for studying enzymatic reactions. First …

Time-dependent dynamical properties of molecules can be quantified with atomic resolution
by using solution-state NMR spectroscopy. A variety of NMR observables, including scalar …

Kinases perform phosphoryl-transfer reactions in milliseconds; without enzymes, these
reactions would take about 8,000 years under physiological conditions. Despite extensive …

Membrane proteins remain difficult to study by traditional methods. Magic angle spinning
solid-state NMR (MAS SSNMR) methods present an important approach for studying …

The enormous rate accelerations observed for many enzyme catalysts are due to strong
stabilizing interactions between the protein and reaction transition state. The defining …

Many enzymes mold their structures to enclose substrates in their active sites such that
conformational remodeling may be required during each catalytic cycle. In adenylate kinase …

Conspectus Biological activities of enzymes, including regulation or coordination of
mechanistic stages preceding or following the chemical step, may depend upon kinetic or …

Triosephosphate isomerase (TIM), glycerol 3-phosphate dehydrogenase, and orotidine 5′-
monophosphate decarboxylase each use the binding energy from the interaction of …

Conformational changes are crucial for the catalytic action of many enzymes. A prototypical
and well-studied example is loop opening and closure in triosephosphate isomerase (TIM) …