Biopolymers and cell. 1989. Volume 5. № 3. 60 - 67

D. B. Dorokhov, V. B. Odintsov, S. V. Kirillov

TEMPLATE-DEPENDENT BINDING OF AMINOACYL-tRNA TO THE A-SITE OF ESCHERICHIA COLI 70S RIBOSOMES IN THE ABSENCE OF TRANSPEPTIDATION

Summary

    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 (A//°~ 11 kcal/mol) and entropy AS0 ——5 cal-mol-'-degree-1. Association constant of Phe-tRNAplRJ measured at 0 °C and during blocking of P-site with a unsplittable ana¬log of peptidyl-tRNA is in good agreement with that dependence.