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 …

Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for
analyzing protein structure, interaction, and dynamics at atomic resolution and in various …

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 …

Internuclear distances represent one of the main structural constraints in molecular structure
determination using solid-state NMR spectroscopy, complementing chemical shifts and …

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

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 …

Structure determination of membrane proteins in native cellular membranes is critical to
precisely reveal their structures in physiological conditions. However, it remains challenging …

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 …