Author(s): Biro JC, Biro JM
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Abstract Transfer RNA molecules (tRNA) have the thermodynamic potential to interact with each other to form dimers (hybridization energy, dG=-33.2±6.7 kcal/mole, compared to the folding energy of the cloverleaf configuration, dG=-25±4.4 kcal/mole, p<0.0001). The dG values have a strong negative correlation with the frequency of co-locations and substitutions of associated amino acids. We suggest that tRNA interactions participate in determining amino acid interactions (co-locations) and consequently the 3D structures of peptides. Copyright © 2012 Elsevier Ltd. All rights reserved.
This article was published in J Theor Biol
and referenced in Journal of Proteomics & Bioinformatics