1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning

T Le Marchand, T Schubeis, M Bonaccorsi… - Chemical …, 2022 - ACS Publications
Since the first pioneering studies on small deuterated peptides dating more than 20 years
ago, 1H detection has evolved into the most efficient approach for investigation of …

How does it really move? Recent progress in the investigation of protein nanosecond dynamics by NMR and simulation

O Stenström, C Champion, M Lehner… - Current Opinion in …, 2022 - Elsevier
Nuclear magnetic resonance (NMR) spin relaxation experiments currently probe molecular
motions on timescales from picoseconds to nanoseconds. The detailed interpretation of …

Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR

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 …

The intriguing molecular dynamics of Cer [EOS] in rigid skin barrier lipid layers requires improvement of the model

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 …

[HTML][HTML] Protein dynamics detected by magic-angle spinning relaxation dispersion NMR

F Napoli, LM Becker, P Schanda - Current Opinion in Structural Biology, 2023 - Elsevier
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 …

A method to construct the dynamic landscape of a bio-membrane with experiment and simulation

AA Smith, A Vogel, O Engberg, PW Hildebrand… - Nature …, 2022 - nature.com
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 …

The Rigid Core and Flexible Surface of Amyloid Fibrils Probed by Magic‐Angle‐Spinning NMR Spectroscopy of Aromatic Residues

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 …

Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR

K Xue, KT Movellan, XC Zhang, EE Najbauer… - Chemical …, 2021 - pubs.rsc.org
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 …

Mechanistic Insights into Microsecond Time-Scale Motion of Solid Proteins Using Complementary 15N and 1H Relaxation Dispersion Techniques

P Rovó, CA Smith, D Gauto, BL de Groot… - Journal of the …, 2019 - ACS Publications
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 …

Recent advances in solid-state relaxation dispersion techniques

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 …