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 …

Membrane proteins perform a host of vital cellular functions. Deciphering the molecular
mechanisms whereby they fulfill these functions requires detailed biophysical and structural …

Proton detection developed in the last 20 years as the method of choice to study
biomolecules in the solid state. In perdeuterated proteins, proton dipolar interactions are …

Disulfide bond formation is fundamentally important for protein structure and constitutes a
key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins …

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 …

Proteins often undergo large-scale conformational transitions, in which secondary and
tertiary structure elements (loops, helices, and domains) change their structures or their …

The interaction of positively charged N‐terminal histone tails with nucleosomal DNA plays
an important role in chromatin assembly and regulation, modulating their susceptibility to …

Large oligomeric enzymes control a myriad of cellular processes, from protein synthesis and
degradation to metabolism. The 0.5 MDa large TET2 aminopeptidase, a prototypical …

Aromatic side chains are important reporters of the plasticity of proteins, and often form
important contacts in protein–protein interactions. We studied aromatic residues in the two …