| Entropy drives the formation of salt bridges in the protein GB3 | |
| Ning Zhang,; Yefei Wang,; Liaoyuan An; Xiangfei Song; Qingshan Huang,; Zhijun Liu; Lishan Yao | |
| 2017-06-19 | |
| 发表期刊 | Angewandte Chemie International Edition
 |
| 卷号 | 56期号:26页码:7601-7604 |
| 产权排序 | (1)Shandong Provincial Key Laboratory of Synthetic Biology Qingdao Institute of Bioenergy and Bioprocess Technology University of Chinese Academy of Sciences;(2)Department National Center for Protein Science Shanghai, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences |
| 摘要 | Salt bridges are very common in proteins. But what drives the formation of protein salt bridges is not clear. In this work, we determined the strength of four salt bridges in the protein GB3 by measuring the DpKa values of the basic residues that constitute the salt bridges with a highly accurate NMR titration method at different temperatures. The results show that the DpKa values increase with temperature, thus indicating that the salt bridges are stronger at higher temperatures. Fitting of DpKa values to the vanQt Hoff equation yields positive DH and DS values, thus indicating that entropy drives salt-bridge formation. Molecular dynamics simulations show that the protein and solvent make opposite contributions to DH and DS. Specifically, the enthalpic gain contributed from the protein is more than offset by the enthalpic loss contributed from the solvent, whereas the entropic gain originates from the desolvation effect. |
| 文章类型 | Article |
| 关键词 | Enthalpy Entropy Nmr Spectroscopy Protein Structures Salt Bridges |
| WOS标题词 | Science & Technology ; Physical Sciences |
| DOI | 10.1002/anie.201702968 |
| 关键词[WOS] | enthalpy ; entropy ; NMR spectroscopy ; protein structures ; salt bridges |
| 收录类别 | SCI |
| 语种 | 英语 |
| 所属项目编号 | 31661143036 ; 31600051 ; 21376254 ; 31600690 |
| WOS研究方向 | Chemistry, Multidisciplinary |
| 项目资助者 | National Natural Science Foundation of China |
| WOS类目 | Chemistry |
| WOS记录号 | WOS:000403017000048 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.qibebt.ac.cn/handle/337004/9710 |
| 专题 | 蛋白质设计研究组 |
| 通讯作者 | Lishan Yao |
| 作者单位 | 1.Shandong Provincial Key Laboratory of Synthetic Biology Qingdao Institute of Bioenergy and Bioprocess Technology University of Chinese Academy of Sciences 2.Department National Center for Protein Science Shanghai, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences |
| 推荐引用方式 GB/T 7714 | Ning Zhang,,Yefei Wang,,Liaoyuan An,et al. Entropy drives the formation of salt bridges in the protein GB3[J]. Angewandte Chemie International Edition,2017,56(26):7601-7604. |
| APA | Ning Zhang,.,Yefei Wang,.,Liaoyuan An.,Xiangfei Song.,Qingshan Huang,.,...&Lishan Yao.(2017).Entropy drives the formation of salt bridges in the protein GB3.Angewandte Chemie International Edition,56(26),7601-7604. |
| MLA | Ning Zhang,,et al."Entropy drives the formation of salt bridges in the protein GB3".Angewandte Chemie International Edition 56.26(2017):7601-7604. |
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| Zhang_et_al-2017-Ang（985KB） | 期刊论文 | 作者接受稿 | 开放获取 | CC BY-NC-SA | 浏览 下载 | |
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