Kinetic measurement of the step size of DNA unwinding by Escherichia coli UvrD helicase

Science

Volumn 275, Issue 5298, 1997, Pages 377-380

  Ali, Janid A ^a   Lohman, Timothy M ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DOUBLE STRANDED DNA; HELICASE;

ARTICLE; BACTERIAL GENETICS; DNA DENATURATION; DNA REPAIR; ENZYME ACTIVITY; ESCHERICHIA COLI; KINETICS; MEASUREMENT; NONHUMAN; PRIORITY JOURNAL;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; BASE COMPOSITION; DNA; DNA HELICASES; DNA, SINGLE-STRANDED; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; NUCLEIC ACID CONFORMATION; OLIGODEOXYRIBONUCLEOTIDES;

EID: 0031031958     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.275.5298.377     Document Type: Article

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23. 2,5 mM 2-mercaptoethanol, 10% (v/v) glycerol, and 0.1 mg/ml bovine serum albumin (BSA). Buffer A is 25 mM tris, pH 7.5, at 25°C, 6 mM NaCl, 5 mM 2-mercaptoethanol, and 10% (v/v) glycerol.
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29. NP to form a productive complex.
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37. We thank I. Wong, K. Bjornson, and K. Moore for critical discussions; M. Amaratunga for preliminary experiments; W. van Zante and T. Ho for DNA synthesis; and P. Burgers, R. Gregorian, and J. Hsieh for comments on the manuscript. Supported in part by NIH grant GM45948.