The Specificity of Peptide Chain Extension by N-Carboxyanhydrides

Details The Specificity of Peptide Chain Extension by N-Carboxyanhydrides The Specificity of Peptide Chain Extension by N-Carboxyanhydrides

Jun 2001

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2001oleb...31..241w&link_type=abstract

Origins of Life and Evolution of the Biosphere, Volume 31, Issue 3, pp.241-248

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Enantiospecificity, N-Carboxyanhydrides, Peptide Elongation

Scientific paper

We have used amino acids activated by carbonyldiimidazole to study the enantiospecificity of peptide elongation in aqueoussolution. Peptide `primers' Glu10 and Ala3Glu10were elongated with the enantiomers of arginine, glutamic acid,asparagine, phenylalanine, serine and valine. The homochiral addition was always the more efficient reaction; the enantiospecificity was large in some cases but very small in others. In every case Ala3Glu10 was elongated more efficiently than Glu10.

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