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- W2000206209 abstract "Isothermal titration calorimetry (ITC), computational, and osmotic stress techniques have been used to characterize the changes in heat capacity, solvent-accessible surface, and hydration that accompany the binding of the aminoglycoside paromomycin to both prokaryotic and eukaryotic rRNA A-site model oligonucleotides. Regarded as a whole, the results of these studies suggest that the intrinsic heat capacity change (ΔCp) for the binding of paromomycin to each rRNA A-site is near zero, with the negative ΔCp observed for the binding of the drug to the prokaryotic rRNA A-site being dictated by the coupled destacking of the adenine residues at positions 1492 and 1493. In this connection, ΔCp provides a useful calorimetric signature for assessing the relative impacts of novel and existing A-site targeting ligands on rRNA conformation, which, in turn, should provide a useful analytical tool for facilitating the drug design process, since aminoglycoside-induced destacking of A1492 and A1493 is thought to be a determining factor in the mistranslational and antimicrobial activities of the drugs." @default.
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- W2000206209 date "2004-10-14" @default.
- W2000206209 modified "2023-09-23" @default.
- W2000206209 title "Deciphering the Origins of Observed Heat Capacity Changes for Aminoglycoside Binding to Prokaryotic and Eukaryotic Ribosomal RNA A-Sites: A Calorimetric, Computational, and Osmotic Stress Study" @default.
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- W2000206209 doi "https://doi.org/10.1021/ja0457516" @default.
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