J-Deconvolution Using Maximum Entropy Reconstruction Applied to 13C-13C Solid-State Cross-Polarization Magic-Angle-Spinning NMR of Proteins
详细信息 查看全文
- 作者：Ingo Scholz ; Stefan Jehle ; Peter Schmieder ; Matthias Hiller ; Frank Eisenmenger ; Hartmut Oschkinat ; Barth-Jan van Rossum
- 刊名：Journal of the American Chemical Society
- 出版年：2007
- 出版时间：May 30, 2007
- 年：2007
- 卷：129
- 期：21
- 页码：6682 - 6683
- 全文大小：49K
- 年卷期：v.129,no.21(May 30, 2007)
- ISSN：1520-5126
文摘
Scalar couplings between 13C spins can impair both resolution and sensitivity in 13C-labeled preparations. It is demonstrated that deconvolution of magic-angle-spinning NMR data with maximum entropy (MaxEnt) reconstruction allows the removal of splittings due to J-couplings without expenses in sensitivity. A combination of MaxEnt reconstruction in t2 with selective pulses in t1 produces fully J-resolved data in both dimensions. The possibility to obtain J-resolved 13C-13C data without compromising the sensitivity is particularly important for solid-state NMR of "difficult" biological samples, like membrane proteins, where sacrifices in signal-to-noise are fatal. The method is demonstrated using preparations of 
-spectrin SH3 domain (62 residues) as small test system and of outermembrane protein G as example of a membrane protein with higher molecular weight (281 residues). Both preparations were obtained using [2-13C]-glycerol as the carbon source during the bacterial growth.
-spectrin SH3 domain (62 residues) as small test system and of outermembrane protein G as example of a membrane protein with higher molecular weight (281 residues). Both preparations were obtained using [2-13C]-glycerol as the carbon source during the bacterial growth.