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 …

Solid-state nuclear magnetic resonance (NMR) spectroscopy is an atomic-level method to
determine the chemical structure, 3D structure and dynamics of solids and semi-solids. This …

Paramagnetic chemical probes have been used in electron paramagnetic resonance (EPR)
and nuclear magnetic resonance (NMR) spectroscopy for more than four decades. Recent …

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 …

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

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 …