ATPase activity of Escherichia coli Rep helicase is dramatically dependent on DNA ligation and protein oligomeric states

Biochemistry

Volumn 35, Issue 18, 1996, Pages 5726-5734

  Wong, Isaac ^a   Moore, Keith J M ^a   Bjornson, Keith P ^a   Hsieh, John ^a   Lohman, Timothy M ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DOUBLE STRANDED DNA; GENE PRODUCT; HELICASE; MONOMER; OLIGODEOXYNUCLEOTIDE; OLIGOMER; SINGLE STRANDED DNA;

ALLOSTERISM; ARTICLE; BINDING SITE; DIMERIZATION; DNA BINDING; DNA DENATURATION; ENZYME ACTIVITY; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION;

ADENOSINE TRIPHOSPHATASES; DNA HELICASES; DNA, BACTERIAL; DNA, SINGLE-STRANDED; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; LIGANDS; MODELS, BIOLOGICAL; PROTEIN BINDING; PROTEIN CONFORMATION;

ESCHERICHIA COLI; FELIS CATUS;

EID: 0029882507     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952959i     Document Type: Article

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