通过 NMR 直接观察蛋白质中的 CH/CH 范德华相互作用。
Direct Observation of CH/CH van der Waals Interactions in Proteins by NMR.
机构信息
University of Chinese Academy of Sciences , Beijing , 100049 , China.
出版信息
J Am Chem Soc. 2018 Mar 7;140(9):3194-3197. doi: 10.1021/jacs.7b13345. Epub 2018 Feb 26.
van der Waals interactions are important to protein stability and function. These interactions are usually identified empirically based on protein 3D structures. In this work, we performed a solution nuclear magnetic resonance (NMR) spectroscopy study of van der Waals interactions by detecting the through-space J-coupling between protein aliphatic side chain groups. Specifically, J-coupling values up to ∼0.5 Hz were obtained between the methyl and nearby aliphatic groups in protein GB3, providing direct experimental evidence for the van der Waals interactions. Quantum mechanical calculations suggest that the J-coupling is correlated with the exchange-repulsion term of van der Waals interaction. NMR detection of J-coupling offers a new tool to characterize such interactions in proteins.
范德华相互作用对蛋白质的稳定性和功能很重要。这些相互作用通常是根据蛋白质的 3D 结构经验性地确定的。在这项工作中，我们通过检测蛋白质脂族侧链基团之间的空间 J 偶联来进行范德华相互作用的溶液核磁共振（NMR）光谱研究。具体来说，在蛋白质 GB3 中，甲基和附近脂族基团之间获得了高达约 0.5 Hz 的 J 偶联值，为范德华相互作用提供了直接的实验证据。量子力学计算表明，J 偶联与范德华相互作用的交换排斥项相关。NMR 检测 J 偶联为在蛋白质中表征此类相互作用提供了一种新工具。
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