The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer

Journal of Biological Chemistry

Volumn 280, Issue 13, 2005, Pages 12221-12230

  Piszczek, Grzegorz ^a,c   Rozycki, Jan ^b,d   Singh, Satyendra K ^b   Ginsburg, Ann ^a   Maurizi, Michael R ^b  

^a Department of Dermatopathology   (United States)

^b NATIONAL CANCER INSTITUTE   (United States)

^c NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^d NONE   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CALORIMETRY; ENZYME INHIBITION; ESCHERICHIA COLI; PH EFFECTS; PROTEINS; SUBSTRATES;

HEXAMER; ISOTHERMAL TITRATION CALORIMETRY (ITC); MOLECULAR CHAPERONE; SUBSTRATE MOTIFS;

POLYPEPTIDES;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CHAPERONE; ENDOPEPTIDASE CLP; ENDOPEPTIDASE CLPA; MAGNESIUM; PROTEINASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; DEGRADATION; DELETION MUTANT; ESCHERICHIA COLI; FLUORESCENCE; ISOTHERMAL TITRATION CALORIMETRY; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MOTIF; STOICHIOMETRY;

EID: 16844376945     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M411733200     Document Type: Article

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