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 …

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 …

With the development of NMR methodology and technology during the past decades, solid-
state NMR (ssNMR) has become a particularly important tool for investigating structure and …

Proton-detected solid-state NMR has emerged as a powerful analytical technique in
structural elucidation via 1H–1H correlations, which are mostly established by broadband …

Solid-state nuclear magnetic resonance (ssNMR) is indispensable for studying the
structures, dynamics, and interactions of insoluble proteins in native or native-like …

With the recent advances in NMR hardware and probe design technology, magic-angle
spinning (MAS) rates over 100​ kHz are accessible now, even on commercial solid NMR …

Solid-state NMR spectroscopy has been playing a significant role in elucidating the
structures and dynamics of materials and proteins at the atomic level for decades. As an …

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 …