Interaction of N-acetyl-phenylalanyl-tRNAPhewith 70S ribosomes of Escherichia coli
Open Access
- 1 October 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 5 (10) , 3871-3880
- https://doi.org/10.1093/nar/5.10.3871
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).Keywords
This publication has 4 references indexed in Scilit:
- [Non-enzymatic specific (codon-dependent) binding of tRNA with isolated 30S ribosomal subunits. Measurement of the dissociation constant of the complex].1975
- [55] The chemical preparation of acetylaminoacyl-tRNAPublished by Elsevier ,1974
- The Elongation Reactions in Protein SynthesisAdvances in Protein Chemistry, 1973
- RNA Codewords and Protein SynthesisScience, 1964