Solid-state NMR analysis of membrane protein complexes with 7-transmembrane helices

固体核磁共振可以在无取向固体中确定生物分子复合物的结构。我们验证了基于偶极和J偶联的魔角自旋固体核磁共振在^<13>C均匀标记生物分子复合物的结构分析中的有效性。我们利用固态核磁共振对脂质双层中的halorhodopshin、mastoparan-X和159- reki传感器蛋白pHtrII进行了研究。固体核磁共振将核磁共振约束与隐式膜环境下的复制交换分子动力学模拟相结合，提供了具有膜的mastoparan-X的详细结构。该方法适用于较大膜蛋白的核磁共振分析。分析了pHtrII移动段的^1H-^<13>C相关性。

Solid-state NMR enables the structural determination of biological molecular complexes in unoriented solids. We verified the usefulness of magic-angle spinning solid-state NMR based on dipolar and J couplings for the structural analysis of ^<13>C uniformly labeled biomolecular complexes. We applied solid-state NMR to halorhodopshin, mastoparan-X and 159-redisue transducer protein pHtrII in lipid bilayers. Solid-state NMR provided the detailed structure of mastoparan-X with membranes by combining NMR constraints with replica exchange molecular dynamics simulation using implicit membrane environment. This method was applied to NMR analysis of larger membrane proteins. ^1H-^<13>C correlations of mobile segments of pHtrII were analyzed.