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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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对NOESY数据的自相对应分析为折叠和展开的蛋白质提供了残留的紧性

Andreas Schedlbauer1, Nicolas Coudevylle, Renate Auer

  • 1Institute of Biomolecular Structural Chemistry, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, A-1030 Vienna, Austria.

Journal of the American Chemical Society
|April 15, 2009
PubMed
概括

这项研究引入了一种新的光谱法,用于使用NOESY数据分析蛋白质结构,而不需要特定的峰值分配. 这种方法揭示了残留物的空间分布,区分灵活和刚性蛋白质区域.

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