Dipolar waves map the structure and topology of helices in membrane proteins
Dipolar waves map the structure and topology of helices in membrane proteins
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DOI：
10.1021/ja034211q
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发表时间：
2003-07-23
影响因子：
15
通讯作者：
Opella, SJ
中科院分区：
文献类型：
--
作者：
Mesleh, MF;Lee, S;Opella, SJ
偶极波描述了膜蛋白的螺旋结构和拓扑结构。理想a-螺旋每转周期3.6个残基的正弦波与偶极耦合实验测量的拟合作为残基数的函数，可以同时识别螺旋中的残基，检测螺旋中的扭曲或曲率，并确定完全排列双层样品中螺旋的绝对旋转和取向以及弱排列胶束样品中共同分子框架中螺旋的相对旋转和取向。由于膜蛋白中多达80%的结构残基是螺旋状的，偶极波的分析为利用核磁共振光谱测定螺旋状膜蛋白的结构提供了重要的一步。
Dipolar waves describe the structure and topology of helices in membrane proteins. The fit of sinusoids with the 3.6 residues per turn period of ideal a-helices to experimental measurements of dipolar couplings as a function of residue number makes it possible to simultaneously identify the residues in the helices, detect kinks or curvature in the helices, and determine the absolute rotations and orientations of helices in completely aligned bilayer samples and relative rotations and orientations of helices in a common molecular frame in weakly aligned micelle samples. Since as much as 80% of the structured residues in a membrane protein are in helices, the analysis of dipolar waves provides a significant step toward structure determination of helical membrane proteins by NMR spectroscopy.