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Updated: Jun 20, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Transverse-dephasing optimized homonuclear j-decoupling in solid-state NMR spectroscopy of uniformly 13C-labeled
Ségolène Laage1, Anne Lesage, Lyndon Emsley
1Université de Lyon, CNRS/ ENS Lyon/ UCB-Lyon 1, Centre RMN à Très Hauts Champs, 5 rue de la Doua, 69100 Villeurbanne, France.
Abstract:
A transverse-dephasing optimized S(3)E (spin-state selective excitation) method is implemented in solid-state NMR experiments of uniformly labeled protein samples, and it is shown to provide a simultaneous significant gain in both resolution (up to a factor of 2.2) and sensitivity (up to a factor of 1.4). This is illustrated with high-resolution NCO and NCA correlations of a microcrystalline sample of the oxidized form of the 153 residue human Cu(II)Zn(II) superoxide dismutase (SOD), a dimeric paramagnetic enzyme of 32 kDa. This method allows the resolution of 145 signals in the highly crowded carbonyl region in the NCO correlation spectrum.
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