Crowding and Confinement Can Oppositely Affect Protein Stability

doi:10.1002/cphc.201800857

	Crowding and Confinement Can Oppositely Affect Protein Stability
	Li, Conggang 2; Liu, Maili 2; Pielak, Gary J.1; Zhang, Zeting 2; Wu, Qiong 2; Cheng, Kai 2
刊名	CHEMPHYSCHEM
	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.
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关键词	NMR-SPECTROSCOPY ; ENCAPSULATION ; THERMODYNAMICS ; STABILIZATION ; COSOLUTES ; CELL
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
内容类型	期刊论文
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.