The benefits of being β-crystallin heteromers: βb1-crystallin protects βa3-crystallin against aggregation during co-refolding

Biochemistry

Volumn 50, Issue 48, 2011, Pages 10451-10461

  Wang, Sha ^a   Leng, Xiao Yao ^a   Yan, Yong Bin ^a  

^a TSINGHUA UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PROCESS; CO-REFOLDING; CRITICAL DETERMINANT; CRYSTALLIN; DIMER INTERFACE; DOSE-DEPENDENT MANNER; FOLDING PATHWAY; IN-VIVO; MONOMERIC INTERMEDIATE; REFOLDING; REFRACTION INDEX; STRUCTURAL PROTEINS; TRANSITION CURVES;

AGGLOMERATION; DIMERS; MAMMALS;

PROTEINS;

BETA CRYSTALLIN; BETA CRYSTALLIN A3; BETA CRYSTALLIN B1; DIMER; MONOMER; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; CONTROLLED STUDY; DIMERIZATION; ENERGY; EQUILIBRIUM CONSTANT; GIBBS FREE ENERGY; KINETICS; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN REFOLDING; PROTEIN STABILITY; SIGNAL TRANSDUCTION; STRESS;

BETA-CRYSTALLIN A CHAIN; BETA-CRYSTALLIN B CHAIN; DIMERIZATION; HUMANS; PROTEIN MULTIMERIZATION; PROTEIN REFOLDING;

EID: 82455175408     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201375p     Document Type: Article

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