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Crowding and Confinement Can Oppositely Affect Protein Stability
Cheng, Kai1; Wu, Qiong1; Zhang, Zeting1; Pielak, Gary J.2; Liu, Maili1; Li, Conggang1
2018-12-19
Source PublicationCHEMPHYSCHEM
ISSN1439-4235
Volume19Issue:24Pages:3350-3355
AbstractProteins 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.
Keywordequilibrium thermodynamics macromolecular crowding NMR spectroscopy protein stability reverse micelles
Funding OrganizationMinistry 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
DOI10.1002/cphc.201800857
WOS KeywordNMR-SPECTROSCOPY ; ENCAPSULATION ; THERMODYNAMICS ; STABILIZATION ; COSOLUTES ; CELL
Language英语
Funding ProjectMinistry 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]
Funding OrganizationMinistry 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
WOS Research AreaChemistry ; Physics
WOS SubjectChemistry, Physical ; Physics, Atomic, Molecular & Chemical
WOS IDWOS:000453765300005
PublisherWILEY-V C H VERLAG GMBH
Citation statistics
Document Type期刊论文
Identifierhttp://ir.wipm.ac.cn/handle/112942/13452
Collection中国科学院武汉物理与数学研究所
Corresponding AuthorLi, Conggang
Affiliation1.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
2.Univ N Carolina, Dept Biochem & Biophys, Dept Chem, Chapel Hill, NC 27599 USA
Recommended Citation
GB/T 7714
Cheng, Kai,Wu, Qiong,Zhang, Zeting,et al. Crowding and Confinement Can Oppositely Affect Protein Stability[J]. CHEMPHYSCHEM,2018,19(24):3350-3355.
APA Cheng, Kai,Wu, Qiong,Zhang, Zeting,Pielak, Gary J.,Liu, Maili,&Li, Conggang.(2018).Crowding and Confinement Can Oppositely Affect Protein Stability.CHEMPHYSCHEM,19(24),3350-3355.
MLA Cheng, Kai,et al."Crowding and Confinement Can Oppositely Affect Protein Stability".CHEMPHYSCHEM 19.24(2018):3350-3355.
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