A dimer of Escherichia coli UvrD is the active form of the helicase in vitro

Journal of Molecular Biology

Volumn 325, Issue 5, 2003, Pages 913-935

  Maluf, Nasib K ^a   Fischer, Christopher J ^a   Lohman, Timothy M ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

DNA unwinding; Helicase II; Mechanism; Repair; Single turnover kinetics

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DIMER; DOUBLE STRANDED DNA; HELICASE; MONOMER; MUTANT PROTEIN; PROTEIN UVRD; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; DNA CLEAVAGE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; ESCHERICHIA COLI; FLOW KINETICS; HYDROLYSIS; IN VITRO STUDY; METHODOLOGY; PRIORITY JOURNAL; PROTEIN DNA BINDING; QUANTITATIVE ANALYSIS; SEQUENCE HOMOLOGY; STOICHIOMETRY;

ESCHERICHIA COLI;

EID: 0037474547     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01277-9     Document Type: Article

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