Enzymatic reactions play a fundamentally important role in controlling and performing most
life processes. 1-3 Thus, understanding how enzymes work has both fundamental and …

Advances in transition state theory and computer simulations are providing new insights into
the sources of enzyme catalysis. Both lowering of the activation free energy and changes in …

Conformational dynamics play a key role in enzyme catalysis. Although protein motions
have clear implications for ligand flux, a role for dynamics in the chemical step of enzyme …

The mechanism of ligand binding coupled to conformational changes in macromolecules
has recently attracted considerable interest. The 2 limiting cases are the “induced fit” …

The ability to make specific perturbations to biological molecules in a cell or organism is a
central experimental strategy in modern research biology. We have developed a general …

Allosteric regulation of protein function is a mechanism by which an event in one place of a
protein structure causes an effect at another site, much like the behavior of a …

▪ Abstract Molecular motions are widely regarded as contributing factors in many aspects of
protein function. The enzyme dihydrofolate reductase (DHFR), and particularly that from …

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

The field of isotope effects has expanded exponentially in the last decade, and researchers
are finding isotopes increasingly useful in their studies. Bringing literature on the subject up …

The thermodynamics and kinetics of the interaction of dihydrofolate reductase (DHFR) with
methotrexate have been studied by using fluorescence, stopped-flow, and single-molecule …