G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment
G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment
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DOI：
10.1073/pnas.0403529101
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发表时间：
2004-06-29
影响因子：
11.1
通讯作者：
Szyperski, T
中科院分区：
文献类型：
--
作者：
Atreya, HS;Szyperski, T
描述了一种基于G-矩阵傅里叶变换（GFT）NMR谱的蛋白质共振归属策略。这里介绍的每个GIFT NMR实验都可以快速提供四维、五维或六维光谱信息，并结合化学位移的精确测量。由此产生的高信息含量，使人们能够获得几乎完整的分配，仅使用四个NMR实验。对于主链酰胺质子检测的“进出”实验，通过使用纵向H-1弛豫优化，数据收集进一步加速到约2.5倍。GFT NMR实验获得的三种蛋白质的分子量范围从8.6至17 kDa，表明所提出的策略是结构基因组学中的自动共振分配的关键利益。
A G-matrix Fourier transform (GFT) NMR spectroscopy-based strategy for resonance assignment of proteins is described. Each of the GIFT NMR experiments presented here rapidly affords four-, five-, or six-dimensional spectral information in combination with precise measurements of chemical shifts. The resulting high information content enables one to obtain nearly complete assignments by using only four NMR experiments. For the backbone amide proton detected "out-and-back" experiments, data collection was further accelerated up to approximate to2.5-fold by use of longitudinal H-1 relaxation optimization. The GFT NMR experiments were acquired for three proteins with molecular masses ranging from 8.6 to 17 kDa, demonstrating that the proposed strategy is of key interest for automated resonance assignment in structural genomics.