Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy
Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy
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DOI：
10.1021/ja078039s
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发表时间：
2008-03-26
影响因子：
15
通讯作者：
Meier, Beat H.
中科院分区：
文献类型：
--
作者：
Manolikas, Theofanis;Herrmann, Torsten;Meier, Beat H.
质子驱动的C-13自旋扩散(PDSD)是一种简单而可靠的二维核磁共振实验。它导致光谱具有高信噪比，其中交叉峰包含关于核间距离的信息。我们表明，总的信息量足以从单一的，统一的C-13，N-15标记的微晶样品中确定一个小蛋白质的原子分辨率结构。以泛素为例，通过手动程序以及手动结构的自动优化以及全自动结构确定方法来确定结构。研究了光谱中核间距与交叉峰强度之间的关系。
Proton-driven C-13 spin diffusion (PDSD) is a simple and robust two-dimensional NMR experiment. It leads to spectra with a high signal-to-noise ratio in which cross-peaks contain information about internuclear distances. We show that the total information content is sufficient to determine the atomic-resolution structure of a small protein from a single, uniformly C-13-, N-15-labeled microcrystalline sample. For the example of ubiquitin, the structure was determined by a manual procedure followed by an automatic optimization of the manual structure as well as by a fully automated structure determination approach. The relationship between internuclear distances and cross-peak intensities in the spectra is investigated.