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- W1992043883 abstract "The method of anticodon loop replacement has been used to make derivatives of yeast tRNAPhe with the substitution at position 37 (tRNAGAAAPhe) and at the anticodon(tRNAGCAGPhe). A quantitative study of the interaction of various types of deacylated yeast tRNAPhe (tRNA+YPhe, tRNAGAAAPhe, tRNA−yPhe) with the P site of the [70S ribosome∗poly(U)]-complex was carried out at different Mg2+ concentrations and temperatures. The presence and nature of the nucleotide situated at the 3′-end of the anticodon are essential for such interaction in E coli ribosomes. Replacement of thee Y base with the unmodified adenosine decreases the interation enthalpy from 39 kcal/mol to 24 kcal/mol, whereas its removal reduces the interaction enthalpy to 16 kcal/mol. Replacement of the second anticodon nucleotide, adenosine, with cytosine further reduces the enthalphy to 6 kcal/mol, which is typical of tRNA-P site interaction in the absence of poly(U). In the absence of poly(U) the affinity of tRNA−YPhe for the P site of the 70S ribosome is five times lower than the affinity of tRNA+YPhe or tRNAGCAGPhe. Thus, in the ribosome the modified nucleotide stabilizes the codon-anticodon interaction through its stacking interaction with the codon-anticodon base stack. In addition, this decreases the free energy of binding as a result of the interaction of the modified nucleotide itself with the hydrophobic center of the P site." @default.
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- W1992043883 date "1994-01-01" @default.
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- W1992043883 title "Effect of the nucleotide-37 on the interaction of tRNAPhe with the P site of Escherichia coli ribosomes" @default.
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- W1992043883 doi "https://doi.org/10.1016/0300-9084(94)90062-0" @default.
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