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- W2091183388 abstract "A 32-residue α-helical peptide with a sequence similiar to that of the GCN4 leucine zipper region is shown to catalyze its own formation by accelerating the amide bond formation of a 17-residue peptide, preactivated as a thiobenzyl ester, and a 15-residue peptide with a N-terminal cysteine. The self-replication process displays parabolic growth characteristics as revealed by a detailed kinetic analysis. Control reactions with single-mutant peptides strongly support a mechanism in which a ternary and/or quaternary complex of the product with both peptide fragments act(s) as the catalytically active intermediate(s). Furthermore, these experiments reveal a remarkable sequence selectivity, as evidenced by the loss of autocatalytic activity as a result of a single replacement of leucine or valine residues with an alanine at the recognition interface." @default.
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- W2091183388 date "1997-07-01" @default.
- W2091183388 modified "2023-10-18" @default.
- W2091183388 title "Peptide Self-Replication Via Template-Directed Ligation" @default.
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- W2091183388 doi "https://doi.org/10.1002/chem.19970030706" @default.
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