The interconversion of conformers of phenylalanyl-tRNA with different affinity to 70S ribosomes of Escherichia coli

Autor:	Vladimir B. Odinzov, S.V. Kirillov
Rok vydání:	1978
Předmět:	Stereochemistry Phenylalanine Kinetics First-order reaction Activation energy medicine.disease_cause Binding constant Molecular Weight RNA Transfer Biochemistry Mole Escherichia coli Genetics medicine Thermodynamics Ribosomes Magnesium ion Conformational isomerism Mathematics
Zdroj:	Nucleic Acids Research. 5:1501-1514
ISSN:	1362-4962 0305-1048
DOI:	10.1093/nar/5.5.1501
Popis:	Earlier the existence of two conformers of Phe-tRNAPhe of E. coli was demonstrated because one of them yields complexes with 70S-poly(U) of extremely high affinity and the other with at least a 105 lower binding constant. We denote the first conformer as HAC (high affinity conformer) and the second as LAC (low affinity conformer). This high difference in binding constants was used for studying the process of reversible interconversion of conformers of Phe-tRNAPhe. The transition kinetics of LAC to HAC in conditions when the latter is stable (in the presence of magnesium ions) was studied and a high value of activation energy (35 kcal/mole) found. The interconversion is the first order reaction and equilibrium does not depend of overall Phe-tRNA concentration.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e70e29ba6db06ddd05aed9a41aefabf https://doi.org/10.1093/nar/5.5.1501 Zobrazit plný text záznamu