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Theoretical conformational analysis on Cyclo(prolyl-phenylalanyl) peptides

✍ Scribed by David Ajò; Gaetano Granozzi; Carlo Di Bello

Publisher
Wiley (John Wiley & Sons)
Year
1977
Tongue
English
Weight
367 KB
Volume
16
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

Empirical energy calculations on cyclo(L‐Pro‐L‐Phe) and cyclo(L‐Pro‐D‐Phe) indicate that different conformations are possible for each molecule. The theoretical results are compared to ir, nmr, and crystallographic data. The interdependence between diketopiperazine ring and side‐chain conformations is also discussed.

📜 SIMILAR VOLUMES

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