Transverse-dephasing optimized homonuclear j-decoupling in solid-state NMR spectroscopy of uniformly 13C-labeled proteins.
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.
Laage
Ségolène
S
Université de Lyon, CNRS/ ENS Lyon/ UCB-Lyon 1, Centre RMN à Très Hauts Champs, 5 rue de la Doua, 69100 Villeurbanne, France.
Lesage
Anne
A
Emsley
Lyndon
L
Bertini
Ivano
I
Felli
Isabella C
IC
Pierattelli
Roberta
R
Pintacuda
Guido
G
D002247:Carbon Isotopes / Q000737:chemistry*; D003460:Crystallization; D009682:Magnetic Resonance Spectroscopy / Q000295:instrumentation / Q000379:methods*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011506:Proteins / Q000737:chemistry*; D013482:Superoxide Dismutase / Q000737:chemistry
D002247:Carbon Isotopes; D011506:Proteins; D013482:Superoxide Dismutase