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

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

The phenomenon of chemical or conformational exchange in NMR spectroscopy has
enabled detailed characterization of time-dependent aspects of biomolecular function …

In every established species, protein-protein interactions have evolved such that they are fit
for purpose. However, the molecular details of the evolution of new protein-protein …

Protein function can be modulated or dictated by the amplitude and timescale of
biomolecular motion, therefore it is imperative to study protein dynamics. Nuclear Magnetic …

Over the last decade amide 15N CEST experiments have emerged as a popular tool to
study protein dynamics that involves exchange between a 'visible'major state and sparsely …

The use of non-uniform sampling of NMR spectra may give significant reductions in the data
acquisition time. For quantitative experiments such as the measurement of spin relaxation …

Molecular dynamics play a significant role in how molecules perform their function. A critical
method that provides information on dynamics, at the atomic level, is NMR-based relaxation …

Background To understand the mechanisms related to the 'dynamical ordering'of
macromolecules and biological systems, it is crucial to monitor, in detail, molecular …

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled
experimentalists to characterize molecular dynamics and kinetics spanning a wide range of …