Specificity in protein-nucleic acid interaction: Part VI--Role of anticodon-amino acid relation on the evolution of present-day protein synthesizing system
Basu, H.S.; Podder, S.K.
Indian Journal of Biochemistry and Biophysics 19(5): 305-308
1982
ISSN/ISBN: 0301-1208 PMID: 7184845 Document Number: 184488
Water-soluble carbodiimide-mediated condensation of the dipeptides Gly-Gly, Gly-L-Tyr, Gly-L-Phe and Gly-L-Leu was carried out in presence of synthetic polynucleotides. The yield of tetrapeptide was more for peptide-nucleotide systems of higher interaction specificity following mainly the anticodon-amino acid relationship described earlier. The product formed had a catalytic effect on the condensation reaction. The racemization of Gly-L-Tyr during condensation was inhibited in the presence of calf thymus DNA. The importance of these findings for understanding pre-biotic evolution of present-day protein synthesizing machinery is discussed.