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

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 …

Protein NMR Spectroscopy: Principles and Practice combines a comprehensive theoretical
treatment of high resolution NMR spectroscopy with an extensive exposition of the …

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 …

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

Contents 1. Introduction................................................................... 63 2. History and
scope............................................................... 71 3. Kinetics and thermodynamics …

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 …

15N relaxation dispersion experiments were applied to the isolated N-terminal SH3 domain
of the Drosophila protein drk (drkN SH3) to study microsecond to second time scale …

It is well-established that dynamics are central to protein function; their importance is
implicitly acknowledged in the principles of the Monod, Wyman and Changeux model of …