Nishida Noritaka, Shimada Ichio
Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo, Japan.
Methods Mol Biol. 2012;757:129-37. doi: 10.1007/978-1-61779-166-6_10.
Specific interactions between proteins are a fundamental process underlying the various biological events, such as cell-cell contacts, signal transduction, and gene expression. Therefore, the structural investigations of protein-protein interactions provide useful information for understanding these events. We describe an NMR method, termed the cross-saturation (CS) method, to determine the binding sites of protein complexes more precisely than conventional NMR methods. The CS method can determine the binding sites of a protein complex that undergoes fast exchange between the free and the bound states, regardless of the molecular size of the complex.
蛋白质之间的特异性相互作用是各种生物事件（如细胞间接触、信号转导和基因表达）背后的基本过程。因此，对蛋白质-蛋白质相互作用的结构研究为理解这些事件提供了有用信息。我们描述了一种核磁共振方法，称为交叉饱和（CS）方法，用于比传统核磁共振方法更精确地确定蛋白质复合物的结合位点。CS方法可以确定在游离态和结合态之间快速交换的蛋白质复合物的结合位点，而不管复合物的分子大小如何。
