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 13C-labeled proteins / S.Laage; A.Lesage; L.Emsley; I.Bertini; I.C.Felli; R.Pierattelli; G.Pintacuda. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - STAMPA. - 131:(2009), pp. 10816-10817. [10.1021/ja903542h]

Transverse-dephasing optimized homonuclear J-decoupling in solid-state NMR spectroscopy of uniformly 13C-labeled proteins

BERTINI, IVANO;FELLI, ISABELLA CATERINA;PIERATTELLI, ROBERTA;
2009

Abstract

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.
131
10816
10817
S.Laage; A.Lesage; L.Emsley; I.Bertini; I.C.Felli; R.Pierattelli; G.Pintacuda
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/368522
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