Interaction of N-acetyl-phenylalanyl-tRNAPhe with 70S ribosomes of escherichia coli

Abstract

The interaction of N-Acetyl-Phe-tRNAPhe with 70 S ribosomes is a reversible process in the absence as well as in the presence of messenger. The equilibrium binding constants of these interactions were measured at different magnesium concentrations and temperatures and thermodynamical quantities computed. The enthalpy of the formation of complexes with the P site of ribosomes is larger by 6,000 cal/mol in the presence of poly (U) than in the presence of poly (C) or in total absence of messenger. Free energy differences are rather small, the association constants differ less than one order of magnitude. The association constant of N-Acetyl-Phe-tRNAPhe with the A site of ribosomes is 30 - 50 times lower than with the P site even in the presence of poly (U). © 1978 Information Retrieval Limited.