Biological macromolecules are highly flexible and continually undergo conformational
fluctuations on a broad spectrum of timescales. It has long been recognized that dynamics …

Biological molecules are often highly dynamic, and this flexibility can be critical for function.
The large range of sampled timescales and the fact that many of the conformers that are …

Solution nuclear magnetic resonance (NMR) spectroscopy is unique in its ability to elucidate
the details of atomic-level structural and dynamical properties of biological macromolecules …

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

The function of bio-macromolecules is determined by both their 3D structure and
conformational dynamics. These molecules are inherently flexible systems displaying a …

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

In the past several decades solution NMR spectroscopy has emerged as a powerful
technique for the study of the structure and dynamics of proteins, providing detailed insights …

Solid-state nuclear magnetic resonance (NMR) spectroscopy has matured to the point that it
is possible to determine the structure of proteins in immobilized states, such as within …

There is growing evidence that structural flexibility plays a central role in the function of
protein molecules. Many of the experimental data come from nuclear magnetic resonance …

NMR spectroscopy is a powerful approach for quantitating molecular conformational
dynamics at multiple atomic sites and over multiple time scales. Extensive studies by …