Abstract:
:The interaction of N--Acetyl--Phe--tRNA Phe 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--tRNA Phe with the A site of ribosomes is 30--50 times lower than with the P site even in the presence of poly (U).
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Odinzov VB,Kirillov SVdoi
10.1093/nar/5.10.3871subject
Has Abstractpub_date
1978-10-01 00:00:00pages
3871-9issue
10eissn
0305-1048issn
1362-4962journal_volume
5pub_type
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