Nuclear magnetic resonance (NMR) spin relaxation experiments currently probe molecular
motions on timescales from picoseconds to nanoseconds. The detailed interpretation of …

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 …

Omega-O-acyl ceramides such as 32-linoleoyloxydotriacontanoyl sphingosine (Cer [EOS])
are essential components of the lipid skin barrier, which protects our body from excessive …

Side-chain motions play an important role in understanding protein structure, dynamics,
protein–protein, and protein–ligand interactions. However, our understanding of protein side …

NMR relaxation dispersion methods provide a holistic way to observe microsecond time-
scale protein backbone motion both in solution and in the solid state. Different nuclei (1H …

Biomolecular function is based on a complex hierarchy of molecular motions. While
biophysical methods can reveal details of specific motions, a concept for the comprehensive …

G protein‐coupled receptors initiate signal transduction in response to ligand binding.
Growth hormone secretagogue receptor (GHSR), the focus of this study, binds the 28 …

This review describes two rotating-frame (R 1 ρ) relaxation dispersion methods, namely the
Bloch-McConnell Relaxation Dispersion and the Near-rotary Resonance Relaxation …

Relaxation in nuclear magnetic resonance is a powerful method for obtaining spatially
resolved, timescale-specific dynamics information about molecular systems. However …

Solid-state near-rotary-resonance measurements of the spin–lattice relaxation rate in the
rotating frame (R 1ρ) is a powerful NMR technique for studying molecular dynamics in the …