Crowding and Confinement Can Oppositely Affect Protein Stability
文献类型:期刊论文
作者 | Li, Conggang2; Liu, Maili2; Pielak, Gary J.1; Zhang, Zeting2; Wu, Qiong2; Cheng, Kai2 |
刊名 | CHEMPHYSCHEM
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出版日期 | 2018-12-19 |
卷号 | 19期号:24页码:3350-3355 |
关键词 | equilibrium thermodynamics macromolecular crowding NMR spectroscopy protein stability reverse micelles |
ISSN号 | 1439-4235 |
DOI | 10.1002/cphc.201800857 |
英文摘要 | Proteins encounter crowded and confined macromolecular milieus in living cells. Simple theory predicts that both environments entropically stabilize proteins if only hard-core repulsive interactions are considered. Recent studies show that chemical interactions between the surroundings and the test protein also play key roles such that the overall effect of crowding or confinement is a balance of hard-core repulsions and chemical interactions. There are, however, few quantitative studies. Here, we quantify the effects of crowding and confinement on the equilibrium unfolding thermodynamics of a model globular protein, KH1. The results do not agree with predictions from simple theory. KH1 is stabilized by synthetic-polymer crowding agents but destabilized by confinement in reverse micelles. KH1 is more entropically stabilized and enthalpically destabilized in concentrated solutions of the monomers than it is in solutions of the corresponding polymers. When KH1 is confined in reverse micelles, the temperature of maximum stability decreases, the melting temperature decreases, and the protein is entropically destabilized and enthalpically stabilized. Our results show the importance of chemical interactions to protein folding thermodynamics and imply that cells utilize chemical interactions to tune protein stability. |
WOS关键词 | NMR-SPECTROSCOPY ; ENCAPSULATION ; THERMODYNAMICS ; STABILIZATION ; COSOLUTES ; CELL |
资助项目 | Ministry of Science and Technology of China[2017YFA0505400] ; 1000 Young Talents Program ; National Natural Science Foundation of China[21575156] ; National Natural Science Foundation of China[21173300] ; US National Science Foundation[MCB 1410854] ; US National Science Foundation[CHE 1607359] |
WOS研究方向 | Chemistry ; Physics |
语种 | 英语 |
WOS记录号 | WOS:000453765300005 |
出版者 | WILEY-V C H VERLAG GMBH |
资助机构 | Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; 1000 Young Talents Program ; 1000 Young Talents Program ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; US National Science Foundation ; US National Science Foundation ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; 1000 Young Talents Program ; 1000 Young Talents Program ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; US National Science Foundation ; US National Science Foundation ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; 1000 Young Talents Program ; 1000 Young Talents Program ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; US National Science Foundation ; US National Science Foundation ; Ministry of Science and Technology of China ; Ministry of Science and Technology of China ; 1000 Young Talents Program ; 1000 Young Talents Program ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; US National Science Foundation ; US National Science Foundation |
源URL | [http://ir.wipm.ac.cn/handle/112942/13451] ![]() |
专题 | 中国科学院武汉物理与数学研究所 |
通讯作者 | Li, Conggang |
作者单位 | 1.Univ N Carolina, Dept Biochem & Biophys, Dept Chem, Chapel Hill, NC 27599 USA 2.Chinese Acad Sci, Collaborat Innovat Ctr Chem Life Sci, Natl Ctr Magnet Resonance Wuhan,Key Lab Magnet Re, Wuhan Inst Phys & Math,State Key Lab Magnet Reson, Wuhan 430071, Hubei, Peoples R China |
推荐引用方式 GB/T 7714 | Li, Conggang,Liu, Maili,Pielak, Gary J.,et al. Crowding and Confinement Can Oppositely Affect Protein Stability[J]. CHEMPHYSCHEM,2018,19(24):3350-3355. |
APA | Li, Conggang,Liu, Maili,Pielak, Gary J.,Zhang, Zeting,Wu, Qiong,&Cheng, Kai.(2018).Crowding and Confinement Can Oppositely Affect Protein Stability.CHEMPHYSCHEM,19(24),3350-3355. |
MLA | Li, Conggang,et al."Crowding and Confinement Can Oppositely Affect Protein Stability".CHEMPHYSCHEM 19.24(2018):3350-3355. |
入库方式: OAI收割
来源:武汉物理与数学研究所
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