High‐resolution solid‐state 13C‐nmr spectra of two series of fully protected oligopeptides, Z‐(Aib)n‐OMe (n = 3−8) and Z‐(Aib)n‐L‐Leu‐(Aib)2‐OMe (n = 0−5), were recorded to gain insight into main‐chain length dependence for 310‐helix formation. We found that all the oligopeptides examined adopt an incipient or a fully developed 310‐helical structure, as judged from the characteristic splitting of the Cβ signals as well as the conformation‐dependent displacements of the Cα and CO peaks. Copyright © 1988 John Wiley & Sons, Inc.
High-resolution Solid-state C-13-nmr of Peptides - A Study of Chain-length Dependence For 310-helix Formation
FORMAGGIO, FERNANDO;TONIOLO, CLAUDIO
1988
Abstract
High‐resolution solid‐state 13C‐nmr spectra of two series of fully protected oligopeptides, Z‐(Aib)n‐OMe (n = 3−8) and Z‐(Aib)n‐L‐Leu‐(Aib)2‐OMe (n = 0−5), were recorded to gain insight into main‐chain length dependence for 310‐helix formation. We found that all the oligopeptides examined adopt an incipient or a fully developed 310‐helical structure, as judged from the characteristic splitting of the Cβ signals as well as the conformation‐dependent displacements of the Cα and CO peaks. Copyright © 1988 John Wiley & Sons, Inc.
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