Biopolym. Cell. 1989; 5(3):60-67.
http://dx.doi.org/10.7124/bc.0000C2
Structure and Function of Biopolymers
Template-dependent binding of aminoacyl-tRNA to the A-site of Escherichia coli 70S ribosomes in the absence of transpeptidation
1Dorokhov D. B., 1Odintsov V. B., 1Kirillov S. V.
  1. B. P. Konstantinov Institute of Nuclear Physics, Academy of Sciences of the USSR
    Gatchina, Leningrad distr., USSR
  2. Institute of Ecological Genetics, Academy of Sciences of the Moldavian SSR
    Kishinev, USSR

Abstract

The equilibrium binding constants of Phe-tRNAPhe to A-site of Escherichia coli ribosomes were measured when the P-site was initially preoccupied by tRNAphe. The temperature dependence of association constant values has permitted calculating enthalpy (ΔH°~ 11 kcal/mol) and entropy ΔS0 – 5 cal-mol-1-degree-1. Association constant of Phe-tRNAplRJ measured at 0 °C and during blocking of P-site with a unsplittable analog of peptidyl-tRNA is in good agreement with that dependence.
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References

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