Nuclear magnetic resonance (NMR) spin relaxation experiments currently probe molecular motions on timescales from picoseconds to nanoseconds. The detailed interpretation of …
L Troussicot, A Vallet, M Molin… - Journal of the …, 2023 - ACS Publications
Disulfide bond formation is fundamentally important for protein structure and constitutes a key mechanism by which cells regulate the intracellular oxidation state. Peroxiredoxins …
F Fandrei, T Havrišák, L Opálka, O Engberg… - Journal of Lipid …, 2023 - ASBMB
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 …
Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing itself as a powerful method for the characterization of protein dynamics at the atomic scale. We discuss …
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 …
LM Becker, M Berbon, A Vallet… - Angewandte Chemie …, 2023 - Wiley Online Library
Aromatic side chains are important reporters of the plasticity of proteins, and often form important contacts in protein–protein interactions. We studied aromatic residues in the two …
Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including …
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 …
P Rovo - Solid State Nuclear Magnetic Resonance, 2020 - Elsevier
This review describes two rotating-frame (R 1 ρ) relaxation dispersion methods, namely the Bloch-McConnell Relaxation Dispersion and the Near-rotary Resonance Relaxation …