ReviewProgress in nuclear magnetic resonance spectroscopy2016
Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.
Review in Progress in nuclear magnetic resonance spectroscopy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.
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111 citing papers in PubMed.
- Controlling the Guanidinium Cation Rotation by Cation-π Interactions.Angewandte Chemie (International ed. in English) · 2026Article
- Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes.Nature chemistry · 2026Article
- Structural and dynamic similarities of nanofibrils and microparticles of engineered spider silk proteins probed by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2026Article
- High-dimensional solid-state NMR facilitated by transverse-mixing optimal control.Research square · 2025Article
- Dynamic structures of a membrane transporter in native cellular membranes.Science advances · 2025Article
- SLEEPY: a comprehensive Python module for simulating relaxation and dynamics in nuclear magnetic resonance.Nature communications · 2025Article
- Solid-state NMR of membrane proteins in situ.Current opinion in structural biology · 2025Review
- Probe design for high sensitivity proton-detected solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2025Article
- Characterization of intrinsically disordered regions through scalar coupling-based solid-state NMR experiments.Biophysics reports · 2025Article
- Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR.Journal of the American Chemical Society · 2025Article
- Dynamics of hydrogen-bonded end groups in bulk polymers revealed by solid-state NMR spectroscopy relaxation dispersion experiments.Communications chemistry · 2025Article
- Proton-Detected Solid-State NMR for Deciphering Structural Polymorphism and Dynamic Heterogeneity of Cellular Carbohydrates in Pathogenic Fungi.Journal of the American Chemical Society · 2025Article
- Temperature-DependentChemistry of materials : a publication of the American Chemical Society · 2025Article
- Solid-state NMR protocols for unveiling dynamics and (drug) interactions of membrane-bound proteins.Protein science : a publication of the Protein Society · 2025Article
- Probing the Dynamics of Yersinia Adhesin A (YadA) in Outer Membranes Hints at Requirements for β-Barrel Membrane Insertion.Journal of the American Chemical Society · 2025Article
- Conformational Dynamics of BacteriochlorophyllThe journal of physical chemistry. B · 2025Article
- OPTO: Automated Optimization for Solid-State NMR Spectroscopy.Journal of the American Chemical Society · 2025Article
- Pseudo rotary resonance relaxation dispersion effects in isotropic samples.Magnetic resonance (Gottingen, Germany) · 2025Article
- Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Review
- Structural and dynamic studies of chromatin by solid-state NMR spectroscopy.Current opinion in structural biology · 2024Review
51 more citing papers are in PubMed but not listed here.
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2 authors.
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Abstract
Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an overview of experimental approaches to study molecular dynamics by MAS solid-state NMR, with an emphasis on the underlying theoretical concepts and differences of MAS solid-state NMR compared to solution-state NMR. The theoretical foundations of nuclear spin relaxation are revisited, focusing on the particularities of spin relaxation in solid samples under magic-angle spinning. We discuss the range of validity of Redfield theory, as well as the inherent multi-exponential behavior of relaxation in solids. Experimental challenges for measuring relaxation parameters in MAS solid-state NMR and a few recently proposed relaxation approaches are discussed, which provide information about time scales and amplitudes of motions ranging from picoseconds to milliseconds. We also discuss the theoretical basis and experimental measurements of anisotropic interactions (chemical-shift anisotropies, dipolar and quadrupolar couplings), which give direct information about the amplitude of motions. The potential of combining relaxation data with such measurements of dynamically-averaged anisotropic interactions is discussed. Although the focus of this review is on the theoretical foundations of dynamics studies rather than their application, we close by discussing a small number of recent dynamics studies, where the dynamic properties of proteins in crystals are compared to those in solution.
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