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- W2049094372 abstract "In order to investigate the hydrogen‐bonding interactions between Escherichia coli ribonuclease HI and the 2′‐hydroxyl functions of the substrate, oligonucleotide duplexes containing 2′‐amino‐2′‐deoxyuridine or 2′‐fluoro‐2′‐deoxyuridine at a specific site were used, and their affinities for the enzyme were determined by kinetic analyses. The results indicate that the hydroxyl groups of the nucleoside 3′‐adjacent to the cleaved phosphodiester linkage and the second nucleoside 5′ to the cleaved phosphodiester act as both a proton donor and an acceptor and as a proton acceptor, respectively, in the enzyme‐substrate complex. A molecular model was constructed using the interactions derived from the results." @default.
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- W2049094372 date "1995-07-17" @default.
- W2049094372 modified "2023-09-26" @default.
- W2049094372 title "Recognition of 2′-hydroxyl groups by<i>Escherichia coli</i>ribonuclease HI" @default.
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- W2049094372 doi "https://doi.org/10.1016/0014-5793(95)00683-z" @default.
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