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

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• 作者：Sgolne Laage ; Anne Lesage ; Lyndon Emsley ; Ivano Bertini ; Isabella C. Felli ; Roberta Pierattelli ; Guido Pintacuda
• 刊名：Journal of the American Chemical Society
• 出版年：2009
• 出版时间：August 12, 2009
• 年：2009
• 卷：131
• 期：31
• 页码：10816-10817
• 全文大小：178K
• 年卷期：v.131,no.31(August 12, 2009)
• ISSN：1520-5126

文摘

A transverse-dephasing optimized S³E (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.