Kinetic and Stoichiometric Analysis for the Binding of Escherichia coli Ribonuclease HI to RNA-DNA Hybrids Using Surface Plasmon Resonance
Open Access
- 1 August 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (35) , 22015-22022
- https://doi.org/10.1074/jbc.272.35.22015
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Studies of the interactions between Escherichia coli ribonuclease HI and its substrateJournal of Molecular Biology, 1994
- Investigating the role of conserved residue Asp134 in Escherichia coli ribonuclease HI by site‐directed random mutagenesisEuropean Journal of Biochemistry, 1994
- Crystal structure of Escherichia coli RNase HI in complex with Mg2+ at 2.8 Å resolution: Proof for a single Mg2+‐binding siteProteins-Structure Function and Bioinformatics, 1993
- Structural details of ribonuclease H from Escherichia coli as refined to an atomic resolutionJournal of Molecular Biology, 1992
- How does RNase H recognize a DNA.RNA hybrid?Proceedings of the National Academy of Sciences, 1991
- Crystal Structure of the Ribonuclease H Domain of HIV-1 Reverse TranscriptaseScience, 1991
- Reconstitution in vitro of RNase H activity by using purified N-terminal and C-terminal domains of human immunodeficiency virus type 1 reverse transcriptase.Proceedings of the National Academy of Sciences, 1991
- Structure of Ribonuclease H Phased at 2 Å Resolution by MAD Analysis of the Selenomethionyl ProteinScience, 1990
- Purification and characterization of the RNase H domain of HIV‐1 reverse transcriptase expressed in recombinant Escherichia coliFEBS Letters, 1990
- Three-dimensional structure of ribonuclease H from E. coliNature, 1990