## Abstract The preparation of the co‐oligopeptides of the series H‐Gly‐Trp‐(Gly)~__n__~‐Trp‐Gly‐OH (__n__ = 0, 1, and 2) and of a number of other unprotected co‐oligopeptides of glycine and tryptophan is reported. The syntheses have been carried out by conventional methods, using, in general, __N_
Co-oligopeptides of glycine and aromatic amino acids with variable distance between the aromatic residues IV. Spectroscopic properties of tryptophan-containing peptides in a cyclohexane phase
✍ Scribed by Arnaldo Dossena; Vincenzo Rizzo; Rosangela Marchelli; Giuseppe Casnati; Pier Luigi Luisi
- Book ID
- 113125046
- Publisher
- Elsevier Science
- Year
- 1976
- Weight
- 770 KB
- Volume
- 446
- Category
- Article
- ISSN
- 0005-2795
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## Abstract The uv absorption and circular dichroism (CD) properties in water (pH 5.9) and trifluoroethanol of several co‐oligopeptides of glycine and tryptophan have been investigated. These compounds contain one tryptophyl residue, such as H‐Gly‐Trp‐OH, H‐Trp‐Gly‐OH, and H‐Gly‐Trp‐Gly‐OH; or two,
## Abstract The preparation of the co‐oligopeptides of the series H‐Gly‐Phe‐(Gly)~__n__~‐Trp‐Gly‐OH (__n__ = 0, 1, 2) and of other free peptides of glycine, L‐tryptophan, and L‐phenylalanine is reported. The syntheses have been carried out by conventional methods, using __N__‐hydroxysuccinimide est
## Abstract The circular dichroic properties of H‐Gly‐Phe‐(Gly)~__n__~‐Trp‐Gly‐OH (II, __n__ = 0,1,2) and of related simpler peptides, such as H‐Phe‐Gly‐OH, H‐Gly‐Phe‐OH, H‐Gly‐Phe‐Gly‐OH, H‐Phe‐Trp‐OH, H‐Phe‐Trp‐Gly‐OH, and H‐Gly‐Phe‐Trp‐OH in water and trifluoroethanol solutions are investigated.
## Abstract Several N‐protected peptide amides, containing two aromatic residues spaced by one glycyl residue, have been enzymatically synthesized starting from P‐Ar‐OH and H‐Gly‐Ar‐NH~2~ (P is the protecting group and Ar is the aromatic residue) and using α‐chymotrypsin as the catalyst for the cou