中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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
出版日期2018-12-19
卷号19期号:24页码:3350-3355
ISSN号1439-4235
关键词equilibrium thermodynamics macromolecular crowding NMR spectroscopy protein stability reverse micelles
DOI10.1002/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
出版者WILEY-V C H VERLAG GMBH
WOS记录号WOS:000453765300005
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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