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- W3119031566 startingPage "101710" @default.
- W3119031566 abstract "Slow timescale dynamics in proteins are essential for a variety of biological functions spanning ligand binding, enzymatic catalysis, protein folding and misfolding regulations, as well as protein-protein and protein-nucleic acid interactions. In this review, we focus on the experimental and theoretical developments of 2H static NMR methods applicable for studies of microsecond to millisecond motional modes in proteins, particularly rotating frame relaxation dispersion (R1ρ), quadrupolar Carr-Purcell-Meiboom-Gill (QCPMG) relaxation dispersion, and quadrupolar chemical exchange saturation transfer NMR experiments (Q-CEST). With applications chosen from amyloid-β fibrils, we show the complementarity of these approaches for elucidating the complexities of conformational ensembles in disordered domains in the non-crystalline solid state, with the employment of selective deuterium labels. Combined with recent advances in relaxation dispersion backbone measurements for 15N/13C/1H nuclei, these techniques provide powerful tools for studies of biologically relevant timescale dynamics in disordered domains in the solid state." @default.
- W3119031566 created "2021-01-18" @default.
- W3119031566 creator A5088220999 @default.
- W3119031566 date "2021-02-01" @default.
- W3119031566 modified "2023-09-26" @default.
- W3119031566 title "Recent developments in deuterium solid-state NMR for the detection of slow motions in proteins" @default.
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- W3119031566 doi "https://doi.org/10.1016/j.ssnmr.2020.101710" @default.
- W3119031566 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7903970" @default.
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