Stoichiometry and DNA Unwinding by the Bacteriophage T4 41:59 Helicase
Open Access
- 1 June 1996
- journal article
- research article
- Published by Elsevier BV
- Vol. 271 (24), 14074-14081
- https://doi.org/10.1074/jbc.271.24.14074
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Bacteriophage T4 Dda Helicase Translocates in a Unidirectional Fashion on Single-stranded DNAPublished by Elsevier BV ,1995
- Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases.Proceedings of the National Academy of Sciences of the United States of America, 1995
- Unwinding of Closed Circular DNA by theEscherichia coliRuvA and RuvB Recombination/Repair ProteinsJournal of Molecular Biology, 1995
- The Phage T4-coded DNA Replication Helicase (gp41) Forms a Hexamer upon Activation by Nucleoside TriphosphatePublished by Elsevier BV ,1995
- Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluorescence energy transferBiochemistry, 1994
- Escherichia coli Rep helicase unwinds DNA by an active mechanismBiochemistry, 1993
- Intrinsically bent DNA.Published by Elsevier BV ,1990
- Energetic coupling between DNA bending and base pair opening.Proceedings of the National Academy of Sciences of the United States of America, 1988
- [61] Rapid kinetic analysis of mechanochemical adenosinetriphosphatasesMethods in Enzymology, 1986
- Bacteriophage T4 DNA replication protein 41. Cloning of the gene and purification of the expressed protein.Published by Elsevier BV ,1985