title: Conformational relationships between amino acids and their anticodons in the primitive decoding system.
abstract: Detailed calculations of the conformational characteristics of a primitive decoding system are presented. A penta-nucleotide serves as the primitive tRNA (PIT) with a triplet of primitive anticodon (PAC) in a helical conformation. This molecular moiety has a cleft in the middle. An amino acid can comfortably nestle into the cleft. The conformation of this molecular association is stabilised by a few hydrogen bonds. The stereochemistry of the moiety restricts the conformational possibilities and the sidechain of the amino acid gets oriented at a proper position and in the correct direction to interact intimately with the PAC in the middle of the PIT. The model favours L-amino acids for beta-D-ribonucleotides. The location of the sidechain of the amino acid in the PIT gives a raison d'être for the important features of the organisation of nucleotide triplets for amino acids in the Genetic Code. The interaction of a few key amino acids with the different combinations of bases as PAC sequences has been studied and the stereochemical basis for the selection of the anticodons for amino acids is elucidated.
mesh_terms: D000596:Amino Acids; D000926:Anticodon; D005075:Biological Evolution; D005815:Genetic Code; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008968:Molecular Conformation; D009690:Nucleic Acid Conformation; D012343:RNA, Transfer
chemical_list: D000596:Amino Acids; D000926:Anticodon; D012343:RNA, Transfer