High-Resolution solid-state 13C-nmr of peptides: A study of chain-length dependence for 310-helix formation

✍ Scribed by Hazime Saitô; Ryoko Tabeta; Fernando Formaggio; Marco Crisma; Claudio Toniolo

• Publisher: Wiley (John Wiley & Sons)
• Year: 1988
• Tongue: English
• Weight: 497 KB
• Volume: 27
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360271006

✦ Synopsis

High-resolution solid-state I3C-nmr spectra of two series of fully protected oligopeptides, Z-(Aib),-OMe ( n = 3-8) and Z-(fib),-L-Leu-(fib),-OMe ( n = 0-5), were recorded to gain insight into main-chain length dependence for 3,0-helix formation. We found that all the oligopeptides examined adopt an incipient or a fully developed 3,,-helical structure, as judged from the characteristic splitting of the C, signals as well as the conformation-dependent displacements of the C, and C=O peaks.