Dissociation of the GroEL-GroES asymmetric complex is accelerated by increased cooperativity in ATP binding to the GRoEL ring distal to GroES

Biochemistry

Volumn 41, Issue 18, 2002, Pages 5938-5944

  Fridmann, Yael ^a   Kafri, Galit ^a   Danziger, Oded ^a   Horovitz, Amnon ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

POSITIVE COOPERATIVITY;

ADENOSINETRIPHOSPHATE; AMINO ACIDS; HYDROLYSIS; MUTAGENESIS; RATE CONSTANTS; REACTION KINETICS; SURFACE PLASMON RESONANCE;

PROTEINS;

ADENOSINE TRIPHOSPHATE; ALANINE; ARGININE; CHAPERONIN; MUTANT PROTEIN;

ARTICLE; CHEMICAL REACTION KINETICS; CONCENTRATION RESPONSE; CONFORMATIONAL TRANSITION; DISSOCIATION; DISSOCIATION CONSTANT; HYDROLYSIS; MATHEMATICAL ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN IMMOBILIZATION; SURFACE PLASMON RESONANCE; WILD TYPE;

ADENOSINE TRIPHOSPHATE; ALLOSTERIC REGULATION; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GROEL PROTEIN; GROES PROTEIN; KINETICS; MACROMOLECULAR SUBSTANCES; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN BINDING;

EID: 0037035552     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi020117v     Document Type: Article

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