Solid-state NMR spectroscopy is one of the most commonly used techniques to study the
atomic-resolution structure and dynamics of various chemical, biological, material, and …

Since the first pioneering studies on small deuterated peptides dating more than 20 years
ago, 1H detection has evolved into the most efficient approach for investigation of …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

Magic-angle spinning solid-state NMR spectroscopy is an important technique to study
molecular structure, dynamics and interactions, and is rapidly gaining importance in …

Biomolecules adopt a dynamic ensemble of conformations, each with the potential to
interact with binding partners or perform the chemical reactions required for a multitude of …

The importance of dynamics to biomolecular function is becoming increasingly clear. A
description of the structure–function relationship must, therefore, include the role of motion …

Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing itself as a
powerful method for the characterization of protein dynamics at the atomic scale. We discuss …

In recent years, exciting developments in instrument technology and experimental
methodology have advanced the field of magic-angle spinning (MAS) nuclear magnetic …

Solid-state NMR (ssNMR) is a technique that allows the study of protein structure and
dynamics at atomic detail. In contrast to X-ray crystallography and cryo-electron microscopy …

Dynamics are intimately linked to protein stability and play a crucial role in important
biological processes, such as ligand binding, allosteric regulation, protein folding, signaling …