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Conformations and properties of the L-tryptophyl-containing peptides in solution, depending on the pH—Theoretical study vs. experiments

✍ Scribed by Bojidarka B. Ivanova; Michael Spiteller

Publisher
Wiley (John Wiley & Sons)
Year
2010
Tongue
English
Weight
720 KB
Volume
93
Category
Article
ISSN
0006-3525

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📜 SIMILAR VOLUMES

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Co-oligopeptides of aromatic amino acids and glycine with a variable distance between the aromatic residues. V. pH-Dependent conformational changes in peptides containing two adjacent tryptophyl residues as evidenced by circular dichroism studies
✍ Vincenzo Rizzo; Pier Luigi Luisi 📂 Article 📅 1977 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 602 KB

## Abstract The influence of pH upon CD spectra of H‐Trp‐Trp‐OH, H‐Trp‐Trp‐Gly‐OH, and H‐Gly‐Trp‐Trp‐OH is investigated and data are compared with those obtained for peptides containing only one tryptophyl residue. A negative Cotton effect at around 225 nm, which in previous work has been related t

Influence of D and L amino-acid residues
Influence of D and L amino-acid residues on the conformation of peptides in solution: A carbon-13 nuclear magnetic resonance study of cyclo(prolyl-leucyl)
✍ Roxanne Deslauriers; Z. Grzonka; Roderich Walter 📂 Article 📅 1976 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 375 KB 👁 2 views

## Abstract The ^13^C chemical shifts and spin‐lattice relaxation times are reported for __cyclo__(L‐Pro‐L‐Leu) and __cyclo__(L‐Pro‐D‐Leu). The chemical shifts of the D and L leucyl residues in the cyclic peptides differ from each other by 1.8 and 3.6 parts per million for the α and β carbons, resp