Solid-state nuclear magnetic resonance structural studies of proteins using paramagnetic probes
Solid-state nuclear magnetic resonance structural studies of proteins using paramagnetic probes
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DOI：
10.1016/j.ssnmr.2012.02.007
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发表时间：
2012-05-01
影响因子：
3.2
通讯作者：
Jaroniec, Christopher P.
中科院分区：
文献类型：
--
作者：
Jaroniec, Christopher P.
通过魔角旋转（MAS）固态NMR光谱法测定生物大分子的三维结构受到与超过5埃的距离对应的基于核偶极耦合的限制的缺乏的阻碍。最近的MAS NMR研究均匀的C-13，N-15-富含蛋白质的顺磁中心已经证明了特定位点的核pseudocontact位移和自旋弛豫增强的测量，其中报告的电子-核距离高达20埃。这些研究为将这种长距离顺磁约束应用于蛋白质结构解析以及固相中蛋白质-蛋白质和蛋白质-配体相互作用的分析铺平了道路。顺磁性物质也有利于快速获取高分辨率和灵敏度的多维固态NMR光谱的生物大分子使用浓缩的数据收集方案，和表征的溶剂可访问的表面的肽和蛋白质。在这篇综述中，我们讨论了魔角旋转核磁共振光谱的一些最新应用，结合顺磁探针的蛋白质结构研究在固态。(C)2012 Elsevier Inc. All rights reserved.
Determination of three-dimensional structures of biological macromolecules by magic-angle spinning (MAS) solid-state NMR spectroscopy is hindered by the paucity of nuclear dipolar coupling-based restraints corresponding to distances exceeding 5 angstrom. Recent MAS NMR studies of uniformly C-13, N-15-enriched proteins containing paramagnetic centers have demonstrated the measurements of site-specific nuclear pseudocontact shifts and spin relaxation enhancements, which report on electron-nucleus distances up to similar to 20 angstrom. These studies pave the way for the application of such long-distance paramagnetic restraints to protein structure elucidation and analysis of protein-protein and protein-ligand interactions in the solid phase. Paramagnetic species also facilitate the rapid acquisition of high resolution and sensitivity multidimensional solid-state NMR spectra of biomacro-molecules using condensed data collection schemes, and characterization of solvent-accessible surfaces of peptides and proteins. In this review we discuss some of the latest applications of magic-angle spinning NMR spectroscopy in conjunction with paramagnetic probes to the structural studies of proteins in the solid state. (C) 2012 Elsevier Inc. All rights reserved.