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 …

This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

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

Internuclear distances represent one of the main structural constraints in molecular structure
determination using solid-state NMR spectroscopy, complementing chemical shifts and …

Protein aggregation is a widespread phenomenon with important implications in many
scientific areas. Although amyloid formation is typically considered as detrimental, functional …

One key bottleneck of solid‐state NMR spectroscopy is that 1H NMR spectra of organic
solids are often very broad due to the presence of a strong network of dipolar couplings. We …

Recently, proton-detected magic-angle spinning (MAS) solid-state nuclear magnetic
resonance (NMR) spectroscopy has become an attractive tool to study the structure and …

Intrinsic disorder is a natural feature of polypeptide chains, resulting in the lack of a defined
three-dimensional structure. Conformational changes in intrinsically disordered regions of a …

Resolution in proton solid state magic angle sample spinning (MAS) NMR is limited by the
intrinsically imperfect nature of coherent averaging induced by either MAS or multiple pulse …

Infectious proteins or prions are a remarkable class of pathogens, where pathogenicity and
infectious state correspond to conformational transition of a protein fold. The conformational …