The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites

Journal of Molecular Biology

Volumn 306, Issue 4, 2001, Pages 889-899

  Schlee, Sandra ^a   Groemping, Yvonne ^a   Herde, Petra ^a   Seidel, Ralf ^a   Reinstein, Jochen ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

Chaperone; ClpB; Disaggregation; Fluorescence; Thermophile

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN; LUCIFERASE; OLIGOMER; PROTEIN CLPB; UNCLASSIFIED DRUG;

ALLOSTERISM; ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; CONSENSUS SEQUENCE; ENZYME ACTIVITY; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN INTERACTION; STEADY STATE; THERMUS THERMOPHILUS;

THERMUS THERMOPHILUS;

EID: 0035793721     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4455     Document Type: Article

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