Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers

Journal of Biological Chemistry

Volumn 288, Issue 24, 2013, Pages 17734-17744

  Sergeeva, Oksana A ^a   Chen, Bo ^b   Haase Pettingell, Cameron ^a   Ludtke, Steven J ^b   Chiu, Wah ^b   King, Jonathan A ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION SUPPRESSION; ATP HYDROLYSIS; CRYO-ELECTRON MICROSCOPY; DOUBLE RING; HIGH MOLECULAR WEIGHT; HOMO-OLIGOMERS; SUBSTRATE RECOGNITION; SUCROSE GRADIENTS;

ELECTRON MICROSCOPES; ESCHERICHIA COLI; HYDROLYSIS; PURIFICATION; SUBSTRATES;

OLIGOMERS;

ADENOSINE TRIPHOSPHATE; CHAPERONIN CCT1 SUBUNIT; CHAPERONIN CCT2 SUBUNIT; CHAPERONIN CCT3 SUBUNIT; CHAPERONIN CCT4 SUBUNIT; CHAPERONIN CCT5 SUBUNIT; CHAPERONIN CCT6 SUBUNIT; CHAPERONIN CCT7 SUBUNIT; CHAPERONIN CCT8 SUBUNIT; CHAPERONIN CONTAINING TCP1; GAMMA CRYSTALLIN; GAMMA D CRYSTALLIN; HOMO OLIGOMER; LUCIFERASE; OLIGOMER; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; COW; CRYOELECTRON MICROSCOPY; ESCHERICHIA COLI; HYDROLYSIS; MALE; MOLECULAR WEIGHT; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN REFOLDING; STAINING; STRUCTURE ANALYSIS;

CCT; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN SELF-ASSEMBLY; PROTEIN-PROTEIN INTERACTIONS; TRIC;

ADENOSINE TRIPHOSPHATE; CENTRIFUGATION, DENSITY GRADIENT; CHAPERONIN 60; CHAPERONIN CONTAINING TCP-1; CHROMATOGRAPHY, GEL; CRYOELECTRON MICROSCOPY; ESCHERICHIA COLI; GAMMA-CRYSTALLINS; HUMANS; HYDROLYSIS; LUCIFERASES; PROTEIN MULTIMERIZATION; PROTEIN REFOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; SERUM ALBUMIN, BOVINE; TRANSITION TEMPERATURE;

BOVINAE; ESCHERICHIA COLI; EUKARYOTA;

EID: 84879059719     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.443929     Document Type: Article

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