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 …

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

We report linewidth and proton T 1, T 1 ρ and T 2′ relaxation data of the model protein
ubiquitin acquired at MAS frequencies up to 126 kHz. We find a predominantly linear …

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 …

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 …

NMR relaxation dispersion methods provide a holistic way to observe microsecond time-
scale protein backbone motion both in solution and in the solid state. Different nuclei (1H …

Proteins perform their functions in solution but their structures are most frequently studied
inside crystals. Here we probe how the crystal packing alters microsecond dynamics, using …

We sequentially assigned the fully-protonated capsids made from core proteins of the
Hepatitis B virus using proton detection at 100 kHz magic-angle spinning (MAS) in 0.7 mm …

Solid‐state NMR spectroscopy has recently enabled structural biology with small amounts of
non‐deuterated proteins, largely alleviating the classical sample production demands. Still …

Magic angle spinning NMR rotating frame relaxation measurements provide a unique
experimental window into biomolecules dynamics, as is illustrated by numerous recent …