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首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Solid-State NMR Shows That Dynamically Different Domains of Membrane Proteins Have Different Hydration Dependence
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Solid-State NMR Shows That Dynamically Different Domains of Membrane Proteins Have Different Hydration Dependence

机译：固态NMR显示动态不同的膜蛋白结构域具有不同的水合依赖性

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摘要

Hydration has a profound influence on the structure, dynamics, and functions of membrane and membrane-embedded proteins. So far the hydration response of molecular dynamics of membrane proteins in lipid bilayers is poorly understood. Here, we reveal different hydration dependence of the dynamics in dynamically different domains of membrane proteins by multidimensional magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy using 121-residue integral diacylglycerol kinase (DAGK) in 1,2-dimyr-istoyl-sn-glycero-3-phosphocholine (DMPC)/l,2-dimyristoyl-sn-glycero-3-phospho-(r-rac-glycerol) (DMPG) lipid bilayers as a model system. The highly mobile and immobile domains of DAGK and their water accessibilities are identified site-spedfically by scalar-and dipolar-coupling based MAS ssNMR experiments, respectively. Our experiments reveal different hydration dependence of the dynamics in highly mobile and immobile domains of membrane proteins. We demonstrate that the fast, large-amplitude motions in highly mobile domains are not triggered until 20% hydration, enhanced at 20—50% hydration and unchanged at above 50% hydration. In contrast, motions on submicrosecond time scale of immobile residues are observed to be independent of the hydration levels in gel phase of lipids, and at the temperature near gel—liquid crystalline phase transition, amplitude of whole-molecule rotations around the bilayer normal is dominated by the fluidity of lipid bilayers, which is strongly hydration dependent. The hydration dependence of the dynamics of DAGK revealed by this study provides new insights into the correlations of hydration to dynamics and function of membrane proteins in lipid bilayers.
机译：水合对膜和膜嵌入蛋白的结构，动力学和功能具有深远的影响。到目前为止，对脂双层中膜蛋白分子动力学的水合作用反应知之甚少。在这里，我们通过在1，2-二甲基-异丁基-sn-甘油-3-磷酸胆碱（DMPC）/ 1,2-二肉豆蔻酰基-sn-甘油-3-磷酸-（r-rac-甘油）（DMPG）脂质双层作为模型系统。通过基于标量和偶极耦合的MAS ssNMR实验分别现场鉴定了DAGK的高迁移和不可迁移域及其水可利用性。我们的实验揭示了膜蛋白的高度可移动和不可移动域中动力学的不同水合依赖性。我们证明，在高度移动的域中快速，大幅度的运动只有在20％的水合作用时才触发，在20-50％的水合作用时增强，而在50％的水合作用时不变。相反，在亚微秒级尺度上，固定残基的运动与脂质凝胶相中的水合水平无关，并且在凝胶-液晶相变附近的温度下，围绕双层法线的全分子旋转幅度占主导地位通过脂质双层的流动性，其高度水合作用。这项研究揭示的DAGK动力学的水合依赖性为脂质双层中水合与膜蛋白的动力学和功能的相关性提供了新的见解。

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