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- W2022210761 abstract "Abstract This paper summarizes our views and data relative to the coevolution of the genetic code and the process of protein synthesis. The component aminoacyl transfer reactions were found to be spontaneous for the most part. However, formation of peptides from phenylalanyl-AMP-ester did not occur, and this observation raises some question as to the mechanism of peptide bond formation in the contemporary. Exploration of properties of amino acids and nucleotides show correlations between both the hydrophobicity and the hydrophilicity of amino acids and their anticodon nucleotides. Furthermore, work with thermal proteinoids shows a possible affinity of amino acids for anticodon nucleotides. We suggest, as a result of these observations, that a primitive protein synthesis system may have existed in which classes of amino acids were activated by mononucleotide triphosphates (i.e., ATP would activate all hydrophobic amino acids, UTP would activate charged hydrophilic amino acids, CTP uncharged hydrophilic amino acids and GTP those of intermediate hydrophobicity). In this model the nucleotidyl triphosphates simultaneously activate and adapt the amino acids. Subsequently, the nucleotide, carrying the amino acid, base pairs with a “messenger” RNA, organizing the amino acids for polymerization. An essential feature of the model is that the recognition step takes place before the “messenger” is present. The mononucleotides are thus envisioned as the simplest evolutionary precursors of tRNAs. Natural selection processes would have led to the evolution from 1/1 coding with mononucleotide adaptors to 3/1 coding via evolution of the tRNAs." @default.
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- W2022210761 title "Genetic coding and protein synthesis: Concerted evolution" @default.
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