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- W2022720648 abstract "Recent advances in biosensor technology have contributed significantly to our understanding of the mechanisms of molecular recognition processes. In this study, a surface plasmon resonance (SPR)-based optical sensor was employed to study the binding interactions between a series of template/primer double-stranded DNA (dsDNA) and DNA polymerase enzymes containing both polymerase and exonuclease activities. The DNA molecules were immobilized on the SPR gold surface by the controlled assembly of a biotinylated phospholipid monolayer, an avidin monolayer, and a layer of biotinylated DNA. By introducing a number of different mismatches at/near the 3‘-end of the primer, the effects of the mismatches on the overall binding affinities of the Klenow fragment (KF) of Escherichia coli DNA polymerase I and T4 and T7 bacteriophage polymerases were measured. While no obvious trend in the overall binding affinity of the Klenow fragment was observed with the introduction of mismatched base pair(s), its polymerase domain ..." @default.
- W2022720648 created "2016-06-24" @default.
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- W2022720648 date "2000-07-13" @default.
- W2022720648 modified "2023-10-16" @default.
- W2022720648 title "Surface Plasmon Resonance Study of DNA Polymerases Binding to Template/Primer DNA Duplexes Immobilized on Supported Lipid Monolayers" @default.
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- W2022720648 doi "https://doi.org/10.1021/la9912951" @default.
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