Proteins are inherently flexible at ambient temperature. At equilibrium, they are
characterized by a set of conformations that undergo continuous exchange within a …

Function in biological systems is exquisitely dependent on spatial and temporal changes in
biomacromolecules. Innumerable biological processes ultimately rely on transduction of …

Ever since its initial development, solution NMR spectroscopy has been used as a tool to
study conformational exchange. Although many systems are amenable to relaxation …

How the interplay between protein structure and internal dynamics regulates protein function
is poorly understood. Often, ligand binding, post-translational modifications and mutations …

Protein function depends on transitions from the ground state to higher energy states.
Deviations from the ground-state structure result from chemical reactivity and conformational …

A long-standing challenge is to understand at the atomic level how protein dynamics
contribute to enzyme catalysis. X-ray crystallography can provide snapshots of …

This review surveys recent investigations of conformational fluctuations of proteins in
solution using NMR techniques. Advances in experimental methods have provided more …

The perspective reviews quantitative investigations of chemical exchange phenomena in
proteins and other biological macromolecules using NMR spectroscopy, particularly …

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

Allosteric regulation is used as a very efficient mechanism to control protein activity in most
biological processes, including signal transduction, metabolism, catalysis and gene …