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 …

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

Hydrogen bonds play integral roles in biological structure, function, and conformational
dynamics and are fundamental to life as it has evolved on Earth. However, our …

This article reviews the large increase in applications of high-resolution 1H magic-angle
spinning (MAS) solid-state NMR, in particular two-dimensional heteronuclear 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 …

Magic-angle spinning (MAS) solid-state NMR becomes an increasingly important tool for the
determination of structures of membrane proteins and amyloid fibrils. Extensive deuteration …

High resolution proton spectra are obtained in MAS solid-state NMR in case samples are
prepared using perdeuterated protein and D2O in the recrystallization buffer. Deuteration …

When applied to biomolecules, solid-state NMR suffers from low sensitivity and resolution.
The major obstacle to applying proton detection in the solid state is the proton dipolar …

In this paper, the intermolecular structural study asserted by the vibrational analysis in the
stretch frequencies of hydrogen bonds (π⋯ H) and dihydrogen bonds (H− δ⋯ H+ δ) have …

In aqueous solutions, the 214-residue low-complexity domain of the FUS protein (FUS-LC)
is known to undergo liquid–liquid phase separation and also to self-assemble into amyloid …