Journal of Proteomics & Bioinformatics
Open Access

Abstract

Quantification of Peptide Bond Types in Human Proteome Indicates How DNA Codons were Assembled at Prebiotic Conditions

Jozef Nahalka

[GADV]-protein world hypothesis [1] leaded me to quantification of decapeptides assembled from G, A, V, D in human proteome. The G, A, V, and D amino acids were related to the nucleotides Guanine (g), Cystosine (c), Uracil (u), and Adenine (a). The search revealed agreement with the genetic code. The types of prebiotic peptide bonds represent probably the first selection power that established the base order in the codons. The genetic code underwent three phases of formation, which explain why modern codons have their particular order of nucleotides: the monobase, dibase and the modern phase (tribase). Sequence alignments and 3D structures of aminoacyl-tRNA synthetases confirm the depicted picture of “relatedness” and the picture indicates how “relatedness” is used by aminoacyl-tRNA synthetases for navigation into and within of the C-terminal anticodon-binding domain. The findings presented here illustrate the novel concept of possible translation of the amino acid sequence into a nucleotide sequence that can be in interactive or contrary mode regarding to desired protein-RNA interactions. Hopefully, it could be used in synthetic biology.