Multistep mechanism of substrate binding determines chaperone activity of Hsp70

Nature Structural Biology

Volumn 7, Issue 7, 2000, Pages 586-593

  Mayer, Matthias P ^a   Schröder, Hartwig ^a,b   Rüdiger, Stefan ^a   Paal, Klaus ^a   Laufen, Thomas ^a   Bukau, Bernd ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b BASF SE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN 70;

ALPHA HELIX; ARTICLE; CONFORMATIONAL TRANSITION; HYDROLYSIS; HYDROPHOBICITY; MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; ALLOSTERIC SITE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; ENZYME ACTIVATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENETIC COMPLEMENTATION TEST; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HYDROLYSIS; KINETICS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MUTATION; PHENOTYPE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SIGMA FACTOR; THERMODYNAMICS; TRANSCRIPTION FACTORS;

EID: 0033936317     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/76819     Document Type: Article

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