Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E. coli RecBCD helicase-catalyzed DNA unwinding

Journal of Molecular Biology

Volumn 339, Issue 4, 2004, Pages 751-771

  Lucius, Aaron L ^a,b   Lohman, Timothy M ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF TEXAS MEDICAL BRANCH   (United States)

Author keywords

ATPase; bp, base pairs; dsDNA, double stranded DNA; FRET; helicase; motor; NLLS, non linear least squares; recombination; ssDNA, single stranded DNA; ME, mercaptoethanol

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; DNA; GLYCEROL; HELICASE; MAGNESIUM CHLORIDE; SODIUM CHLORIDE;

ARTICLE; CATALYSIS; DNA DENATURATION; ESCHERICHIA COLI; FLOW KINETICS; FLUORESCENCE; FLUORESCENCE RESONANCE ENERGY TRANSFER; MONITORING; NONHUMAN; PH; PRIORITY JOURNAL; TEMPERATURE SENSITIVITY;

ESCHERICHIA COLI;

EID: 2542475076     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.04.010     Document Type: Article

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38. this issue Lucius A.L., Wong C.J., Lohman T.M. Fluorescence stopped-flow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding. J. Mol. Biol. 339:2004