The oligomeric structure of GroEL/GroES is required for biologically significant chaperonin function in protein folding

Nature Structural Biology

Volumn 5, Issue 11, 1998, Pages 977-985

  Weber, Frank ^a   Keppel, France ^b   Georgopoulos, Costa ^b   Hayer Hartl, Manajit K ^a   Hartl, F Ulrich ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b UNIVERSITY OF GENEVA MEDICAL SCHOOL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; MUTANT PROTEIN; OLIGOMER; POLYPEPTIDE;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE;

ANIMALS; CATTLE; CIRCULAR DICHROISM; CITRATE (SI)-SYNTHASE; ESCHERICHIA COLI; GENETIC COMPLEMENTATION TEST; GROEL PROTEIN; GROES PROTEIN; MALATE DEHYDROGENASE; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SEQUENCE DELETION; TETRAHYDROFOLATE DEHYDROGENASE; THIOSULFATE SULFURTRANSFERASE;

ESCHERICHIA COLI;

EID: 0031791650     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/2952     Document Type: Article

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