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- W2017884036 abstract "Abstract The manual dansyl-Edman 1 degradation procedure is one of the most convenient and widely used techniques for the sequencing of peptides up to about 15 residues in length (1,2). A frequently encountered complication in this procedure is the resistance of certain peptide bonds to acid hydrolysis. If the amino terminal peptide bond of the dansylated peptide is especially resistant, the dansyl dipeptide is frequently in higher yield than the corresponding dansyl amino acid. The resistant dansyl dipeptide is often composed of two hydrophobic amino acid residues. The resistance of such peptide bonds to acid hydrolysis is well understood (3). Other resistant bonds have, however, been noted in practice, e.g., those involving a hydrophobic and a prolyl residue. This phenomenon can lead to difficulty in interpretation of the thin-layer chromatogram and to subsequent incorrect identification of amino acid residues. Extending the hydrolysis time to 24 hr still leaves especially resistant dipeptides as the major product while significantly reducing the yield of other dansylated residues, notably dansyl proline, serine, and threonine. We report here the chromatographic behavior of 18 dansyl dipeptides on polyamide thin-layers using the solvent systems commonly employed in the dansyl-Edman procedure (2). All of these dipeptides have been encountered in practice, and the extent of hydrolysis in 6 n HCl at 110°C is usually less than 20%." @default.
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- W2017884036 date "1978-07-01" @default.
- W2017884036 modified "2023-09-26" @default.
- W2017884036 title "Identification of dansyl dipeptides in the dansyl-Edman peptide degradation" @default.
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- W2017884036 doi "https://doi.org/10.1016/0003-2697(78)90431-1" @default.
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