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 …

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 …

Solid-state NMR spectroscopy has developed into a useful method for protein structure
determination. In contrast to diffraction methods, NMR spectroscopy does not rely on long …

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 …

In this chapter, we summarize the isotopic labeling strategies used to obtain high-quality
solution and solid-state NMR spectra of biological samples, with emphasis on integral …

A novel deuterium-excited and proton-detected quadruple-resonance three-dimensional
(3D) 2 H α c α NH MAS nuclear magnetic resonance (NMR) method is presented to obtain …

The structural and dynamical characterization of membrane proteins in a lipid bilayer at
physiological pH and temperature and free of crystal constraints is crucial for the elucidation …

We describe a 2 H based MAS nuclear magnetic resonance (NMR) method to obtain site-
specific molecular dynamics of biomolecules. The method utilizes the use of deuterium …

Nuclear magnetic resonance (NMR) spectroscopy is a principal well-established technique
for analysis of chemical, biological, food and environmental samples. This article provides …

Many advances in instrumentation and methodology have furthered the use of solid-state
NMR as a technique for determining the structures and studying the dynamics of molecules …