Balance of ATPase stimulation and nucleotide exchange is not required for efficient refolding activity of the DnaK chaperone

FEBS Letters

Volumn 579, Issue 25, 2005, Pages 5713-5717

  Groemping, Yvonne ^a   Seidel, Ralf ^a,b   Reinstein, Jochen ^a  

^a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

^b MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

Author keywords

Chaperone; DNAK system; Folding; Kinetics; Regulation

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; NUCLEOTIDE; PROTEIN DNAJ; PROTEIN DNAK;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; STATISTICAL SIGNIFICANCE; THERMUS THERMOPHILUS;

ADENOSINE TRIPHOSPHATASES; BACTERIAL PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HYDROLYSIS; LUCIFERASES; NUCLEOTIDES; PROTEIN FOLDING; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; THERMUS THERMOPHILUS;

EID: 26844446468     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.09.056     Document Type: Article

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