Hydrolysable ATP is a requirement for the correct interaction of molecular chaperonins cpn60 and cpn10

Biochemical Journal

Volumn 364, Issue 3, 2002, Pages 849-855

  Walters, Chris ^a   Errington, Neil ^a   Rowe, Arther J ^a   Harding, Stephen E ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

Analytical ultracentrifugation; ATP S ; Dynamic light scattering; Hydrodynamic bead modelling

Indexed keywords

ABSORPTION; HYDRODYNAMICS; HYDROLYSIS; SPECTROPHOTOMETRY;

BINDING ABILITIES;

ADENOSINETRIPHOSPHATE;

ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONIN;

ABSORPTION SPECTROPHOTOMETRY; ARTICLE; DISSOLUTION; ENZYME INHIBITION; HYDRODYNAMICS; HYDROLYSIS; LIGHT SCATTERING; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SEDIMENTATION RATE; ULTRACENTRIFUGATION;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; CHAPERONIN 10; CHAPERONIN 60; ESCHERICHIA COLI; GROEL PROTEIN; GROES PROTEIN; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; PROTEIN CONFORMATION;

EID: 0037097031     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20011643     Document Type: Article

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