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 …

The field of paramagnetic NMR has expanded considerably in recent years. This review
addresses both the theoretical description of paramagnetic NMR, and the way in which it is …

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

Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has
focused on highly deuterated samples, in which only a small number of protons are …

Using a set of six 1H-detected triple-resonance NMR experiments, we establish a method for
sequence-specific backbone resonance assignment of magic angle spinning (MAS) nuclear …

Solid‐state NMR spectroscopy is an emerging tool for structural studies of crystalline,
membrane‐associated, sedimented, and fibrillar proteins. A major limitation for many studies …

Magic angle spinning (MAS) nuclear magnetic resonance (NMR) has evolved significantly
over the past three decades and established itself as a vital tool for the structural analysis of …

Magic-angle spinning (MAS) is a technique that is a prerequisite for high-resolution solid-
state NMR spectroscopy of proteins and other biomolecules. Recently, the 100 kHz limit for …

When combined with high-frequency (currently∼ 60 kHz) magic-angle spinning (MAS),
proton detection boosts sensitivity and increases coherence lifetimes, resulting in narrow 1 …