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 …

Macromolecular function frequently requires that proteins change conformation into high-
energy states,,–. However, methods for solving the structures of these functionally essential …

A unique feature of chemical catalysis mediated by enzymes is that the catalytically reactive
atoms are embedded within a folded protein. Although current understanding of enzyme …

We used nuclear magnetic resonance relaxation dispersion to characterize higher energy
conformational substates of Escherichia coli dihydrofolate reductase. Each intermediate in …

NMR spectroscopy is a powerful tool for biologists interested in the structure, dynamics, and
interactions of biological macromolecules. This review aims at presenting in an accessible …

Nuclear magnetic resonance (NMR) is widely used across many fields of science because
of the rich data it produces, and some of the most valuable data come from studies of …

Protein-folding intermediates have been implicated in amyloid fibril formation involved in
neurodegenerative disorders. However, the structural mechanisms by which intermediates …

Molecular dynamics are essential for protein function. In some cases these dynamics involve
the interconversion between ground state, highly populated conformers and less populated …

Myriad biological processes proceed through states that defy characterization by
conventional atomic-resolution structural biological methods. The invisibility of these …