A study of a C α, β ‐didehydroalanine homo‐oligopeptide series in the solid‐state by 13 C cross‐polarization magic angle spinning NMR

A study of a C α, β ‐didehydroalanine homo‐oligopeptide series in the solid‐state by 13 C cross‐polarization magic angle spinning NMR

The fully extended peptide conformation (2.0 5 ‐helix) has been investigated for the first time in the solid‐state by 13 C cross‐polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo‐oligopeptide series (from monomer through hexamer) based on C α,...

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Veröffentlicht in:Journal of peptide science 2004-06, Vol.10 (6), p.336-341
Hauptverfasser: Henzler Wildman, Katherine A., Ramamoorthy, Ayyalusamy, Wakamiya, Tateaki, Yoshikawa, Taichi, Crisma, Marco, Toniolo, Claudio, Formaggio, Fernando
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Sprache:eng
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Zusammenfassung:The fully extended peptide conformation (2.0 5 ‐helix) has been investigated for the first time in the solid‐state by 13 C cross‐polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo‐oligopeptide series (from monomer through hexamer) based on C α, β ‐didehydroalanine. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.551