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 …

The dynamics of proteins in solution includes a variety of processes, such as backbone and
side-chain fluctuations, interdomain motions, as well as global rotational and translational …

Detailed descriptions of atomic coordinates and motions are required for an understanding
of protein dynamics and their relation to molecular recognition, catalytic function, and …

The power of combining sum frequency generation (SFG) vibrational spectroscopy and solid-
state nuclear magnetic resonance (ssNMR) spectroscopy to quantify, with site specificity and …

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 …

Previously, Ishii et al., could show that chelated paramagnetic ions can be employed to
significantly decrease the recycle delay of a MAS solid-state NMR experiment [NP …

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 …

A reliable site-specific estimate of the individual N− H bond lengths in the protein backbone
is the fundamental basis of any relaxation experiment in solution and in the solid-state NMR …

In this paper, we seek to compare the internal dynamics of a small globular protein, SH3
domain from α-spectrin, in solution and in a crystalline state. The comparison involves side …