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Title:
Entropy drives the formation of salt bridges in the protein GB3
Author: Ning Zhang,; Yefei Wang,; Liaoyuan An; Xiangfei Song; Qingshan Huang,; Zhijun Liu; Lishan Yao
Source: Angewandte Chemie International Edition
Issued Date: 2017-06-19
Volume: 56, Issue:26, Pages:7601-7604
Keyword: enthalpy ; entropy ; NMR spectroscopy ; protein structures ; salt bridges
DOI: 10.1002/anie.201702968
Corresponding Author: Lishan Yao
DOC Type: Article
English Abstract: 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.
WOS Headings: Science & Technology ; Physical Sciences
WOS Subject: Chemistry
WOS Subject Extended: Chemistry, Multidisciplinary
WOS Keyword Plus: enthalpy ;  entropy ;  NMR spectroscopy ;  protein structures ;  salt bridges
Indexed Type: SCI
Project Number: 31661143036  ; 31600051  ; 21376254 ; 31600690
Funder: National Natural Science Foundation of China
Language: 英语
WOS ID: WOS:000403017000048
Rank: (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
Citation statistics:
Content Type: 期刊论文
URI: http://ir.qibebt.ac.cn/handle/337004/9710
Appears in Collections:仿真与模拟团队_期刊论文

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description.institution: 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

Recommended Citation:
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.
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