Transverse-Dephasing Optimized Homonuclear J-Decoupling in Solid-State NMR Spectroscopy of Uniformly C-13-Labeled Proteins

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A transverse-dephasing optimized (SE)-E-3 (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.

Transverse-Dephasing Optimized Homonuclear J-Decoupling in Solid-State NMR Spectroscopy of Uniformly C-13-Labeled Proteins

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Multimodal Response to Copper Binding in Superoxide Dismutase Dynamics

A Factor Two Improvement in High-Field Dynamic Nuclear Polarization from Gd(III) Complexes by Design

NMR spectroscopy of single sub-nL ova with inductive ultra-compact single-chip probes

Multimodal Response to Copper Binding in Superoxide Dismutase Dynamics

A Factor Two Improvement in High-Field Dynamic Nuclear Polarization from Gd(III) Complexes by Design

NMR spectroscopy of single sub-nL ova with inductive ultra-compact single-chip probes