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 …

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 …

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 …

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 …

NMR chemical shifts provide detailed information on the chemical properties of molecules,
thereby complementing structural data from techniques like X-ray crystallography and …

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 …

Spectral resolution is the key to unleashing the structural and dynamic information contained
in NMR spectra. Fast magic‐angle spinning (MAS) has recently revolutionized the …