We present a protocol for the experimental determination of ensembles of protein
conformations that represent simultaneously the native structure and its associated …

Interactions between proteins are central to biology and are becoming increasingly
important targets for drug design. Upon forming complexes, protein conformations usually …

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The article focuses on the importance of using nuclear magnetic resonance (NMR)
spectroscopy to determine the structures of small proteins in the US Peter Wright, a protein …

Globular proteins in the native state undergo small-amplitude conformational fluctuations1,
which can be observed experimentally, for example, as temperature factors in X-ray …

Because proteins are central to cellular function, researchers have sought to uncover the
secrets of how these complex macromolecules execute such a fascinating variety of …

Molecular dynamics—the science of simulating the motions of a system of particles—applied
to biological macromolecules gives the fluctuations in the relative positions of the atoms in a …

The polypeptide chains that make up proteins have thousands of atoms and hence millions
of possible inter-atomic interactions. It might be supposed that the resulting complexity …

Nuclear magnetic resonance spectroscopy is transforming our views of proteins by revealing
how their structures and dynamics are closely intertwined to underlie their functions and …

Internal motion is central to protein folding, to protein stability through the resulting residual
entropy, and to protein function,,,,,. Despite its importance, the precise nature of the internal …