Protein-Inhibitor Interaction Studies Using NMR.
Protein-Inhibitor Interaction Studies Using NMR.
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DOI：
10.2174/9781608059621115010007
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Ishima R
中科院分区：
文献类型：
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作者：
Ishima R
溶液态核磁共振已被广泛应用于确定蛋白质的三维结构，动力学和分子相互作用。蛋白质NMR中使用的实验设计与小分子NMR中使用的实验设计不同，主要是因为实验前可用的信息，如分子量和一级结构的知识，与小分子相比，蛋白质是独特的。在这篇评论文章中，蛋白质NMR结构生物学的介绍与小分子NMR的比较，如标记策略的描述和分子动力学对弛豫的影响。接下来，蛋白质NMR的应用进行了综述，特别是蛋白质观察配体蛋白质相互作用研究的实际方面。总体而言，以下主题被描述：（1）蛋白质NMR的特性，（2）通过NMR检测蛋白质-配体相互作用的方法，和（3）进行蛋白质-观察到的配体-蛋白质相互作用研究的实践方面。
Solution-state NMR has been widely applied to determine the three-dimensional structure, dynamics, and molecular interactions of proteins. The designs of experiments used in protein NMR differ from those used for small-molecule NMR, primarily because the information available prior to an experiment, such as molecular mass and knowledge of the primary structure, is unique for proteins compared to small molecules. In this review article, protein NMR for structural biology is introduced with comparisons to small-molecule NMR, such as descriptions of labeling strategies and the effects of molecular dynamics on relaxation. Next, applications for protein NMR are reviewed, especially practical aspects for protein-observed ligand-protein interaction studies. Overall, the following topics are described: (1) characteristics of protein NMR, (2) methods to detect protein-ligand interactions by NMR, and (3) practical aspects of carrying out protein-observed inhibitor-protein interaction studies.