Identifying and studying ubiquitin receptors by NMR.
Identifying and studying ubiquitin receptors by NMR.
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通过NMR识别和研究泛素受体。
DOI：
10.1007/978-1-61779-474-2_20
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Walters KJ
中科院分区：
文献类型：
--
作者：
Chen X;Walters KJ
泛素和泛素链被一个庞大且不断增长的受体蛋白家族所识别。核磁共振波谱提供了一种强大的手段来评估蛋白质是否以及如何与泛素结合。它可以用来测量结合亲和力，绘制相互作用表面，并解算泛素：受体复合体的三维结构。在这里，我们描述了三种不同复杂性的核磁共振技术，它们是表征蛋白质的有价值的工具：蛋白质复合体。这些实验包括异核关联实验，通过自旋标记的顺磁弛豫增强(PRE)实验，以及通过核Overhauser效应(NOE)获得分子间偶极-偶极相互作用的技术。
Ubiquitin and ubiquitin chains are recognized by a large and growing family of receptor proteins. NMR spectroscopy provides a powerful means to evaluate whether and how a protein binds to ubiquitin. It can be used to measure binding affinities, to map interaction surfaces, and to solve the three-dimensional structure of ubiquitin:receptor complexes. Herein, we describe three NMR techniques of varying complexity that are valuable tools to characterize protein:protein complexes. These include heteronuclear correlation experiments, paramagnetic relaxation enhancement (PRE) experiments via spin labeling, and techniques designed to obtain intermolecular dipole–dipole interactions by nuclear Overhauser effects (NOEs).