Mapping protein-protein interactions in solution by NMR Spectroscopy
Mapping protein-protein interactions in solution by NMR Spectroscopy
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DOI：
10.1021/bi011870b
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发表时间：
2002-01-08
期刊：
影响因子：
2.9
通讯作者：
Zuiderweg, ERP
中科院分区：
文献类型：
--
作者：
Zuiderweg, ERP
NMR非常适合研究特别弱蛋白 - 蛋白质相互作用，因为不需要结晶。审查并用最近的生化文献中的应用来审查并说明了该末端的NMR方法：分子间NOE，交叉饱和，化学移动扰动，动态和交换扰动，顺磁方法和偶极方向。这些方法中的大多数现在通常适用于总分子质量为60 kDa的复合物，并且可以应用于最高1000 kDa的系统。所研究的大量复合物显示出诱导的拟合的明显影响，影响了接触界面以外的结构和动力学特性。
NMR is very well suited to the study of especially weak protein-protein interactions, as no crystallization is required. The available NMR methods to this end are reviewed and illustrated with applications from the recent biochemical literature: intermolecular NOEs, cross-saturation, chemical shift perturbation, dynamics and exchange perturbation, paramagnetic methods, and dipolar orientation. Most of these methods are now routinely applied for complexes with total molecular mass of 60 kDa and can likely be applied to systems up to 1000 kDa. A substantial fraction of complexes studied show distinct effects of induced fit affecting structural and dynamical properties beyond the contact interface.