Protein dynamics detected by magic-angle spinning relaxation dispersion NMR Napoli, Federico ; https://orcid.org/0000-0002-9043-136X Becker, Lea Marie ; https://orcid.org/0000-0002-6401-5151 Schanda, Paul ; https://orcid.org/0000-0002-9350-7606 ddc:570 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 here how R1ρ MAS relaxation dispersion NMR can explore microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling, and pulse sequence design has paved the way for quantitative analyses of even rare structural fluctuations. In addition to isotropic chemical-shift fluctuations exploited in solution-state NMR relaxation dispersion experiments, MAS NMR has a wider arsenal of observables, allowing to see motions even if the exchanging states do not differ in their chemical shifts. We demonstrate the potential of the technique for probing motions in challenging large enzymes, membrane proteins, and protein assemblies. Elsevier 2023 info:eu-repo/semantics/article doc-type:article article http://purl.org/coar/resource_type/c_2df8fbb1 https://research-explorer.ista.ac.at/record/14036 https://research-explorer.ista.ac.at/download/14036/14907 Napoli F, Becker LM, Schanda P. Protein dynamics detected by magic-angle spinning relaxation dispersion NMR. <i>Current Opinion in Structural Biology</i>. 2023;82(10). doi:<a href="https://doi.org/10.1016/j.sbi.2023.102660">10.1016/j.sbi.2023.102660</a> eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.sbi.2023.102660 info:eu-repo/semantics/altIdentifier/issn/0959-440X info:eu-repo/semantics/altIdentifier/e-issn/1879-033X info:eu-repo/semantics/altIdentifier/wos/001053616200001 info:eu-repo/semantics/altIdentifier/pmid/37536064 info:eu-repo/semantics/openAccess