Specificity of protein - Nucleic acid interaction and the biochemical evolution


Autoria(s): Podder, SK; Basu, HS
Data(s)

01/12/1984

Resumo

The water soluble carbodiimide mediated condensation of dipeptides of the general form Gly-X was carried out in the presence of mono- and poly-nucleotides. The observed yield of the tetrapeptide was found to be higher for peptide-nucleotide system of higher interaction specificity following mainly the anticodon-amino acid relationship (Basu, H.S. & Podder, S.K., 1981, Ind. J. Biochem. Biophys.,19, 251-253). The yield of the condensation product of L-peptide was more because of its higher interaction specificity. The extent of the racemization during the condensation of Gly-L-Phe, Gly-L-Tyr and Gly-D-Phe was found to be dependent on the specificity of the interaction -the higher the specificity, the lesser the racemization. The product formed was shown to have a catalytic effect on the condensation reaction. These data thus provide a mechanism showing how the specific interaction between amino acids/dipeptides and nucleic acids could lead to the formation of the lsquoprimitiversquo translation machinery.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/22884/1/3.pdf

Podder, SK and Basu, HS (1984) Specificity of protein - Nucleic acid interaction and the biochemical evolution. In: Origins of Life and Evolution of Biospheres, 14 (1-4). pp. 477-484.

Publicador

Springer

Relação

http://www.springerlink.com/content/n517106410081157/

http://eprints.iisc.ernet.in/22884/

Palavras-Chave #Biochemistry
Tipo

Journal Article

PeerReviewed