• 1 January 1984
    • journal article
    • research article
    • Vol. 24  (5) , 421-429
Abstract
The conformational features of Boc-Asn-NHMe, Boc-Asn-Gly-NHMe, Boc-Gly-Asn-NHMe and their glycosylated derivatives were studied using NMR spectroscopy. From the temperature dependence of the amide proton chemical shifts and vicinal coupling constants, little change was confirmed in the peptide conformation upon N-glycosylation. There is no particular intramolecular interaction between the peptide and carbohydrate moieties. Boc-Asn-Gly-NHMe takes, to some extent, a folded structure with a hydrogen bond involving the amide proton of N-methylamide group. This backbone conformation is also preferable in the corresponding glycopeptide.