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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
Source PublicationAngewandte Chemie International Edition
Volume56Issue:26Pages:7601-7604
Contribution 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
AbstractSalt 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.
SubtypeArticle
KeywordEnthalpy Entropy Nmr Spectroscopy Protein Structures Salt Bridges
WOS HeadingsScience & Technology ; Physical Sciences
DOI10.1002/anie.201702968
WOS Keywordenthalpy ;  entropy ;  NMR spectroscopy ;  protein structures ;  salt bridges
Indexed BySCI
Language英语
Project Number31661143036  ; 31600051  ; 21376254 ; 31600690
WOS Research AreaChemistry, Multidisciplinary
Funding OrganizationNational Natural Science Foundation of China
WOS SubjectChemistry
WOS IDWOS:000403017000048
Citation statistics
Cited Times:4[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qibebt.ac.cn/handle/337004/9710
Collection蛋白质设计研究组
Corresponding AuthorLishan Yao
Affiliation1.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
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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