(1)H NMR studies of hydroxy protons of the V[beta-Gal(1-->3)-alpha-GalNAc(1-->O)]THPGY glycopeptide. |
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Authors: | L Kindahl C Sandstr?m T Norberg L Kenne |
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Affiliation: | Department of Chemistry, Swedish University of Agricultural Sciences, PO Box 7015, SE 750 07 Uppsala, Sweden. |
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Abstract: | The hydroxy protons of the disaccharide moiety in the glycopeptide Val-[beta-Gal(1-->3)-alpha-GalNAc(1-->O)]-Thr-His-Pro-Gly-Tyr (1) have been investigated in aqueous solution using (1)H NMR spectroscopy. The chemical shifts (delta), coupling constants ((3)J(CH,OH)), temperature coefficients (d delta/dT), exchange rates (k(ex)), and NOEs have been measured. The data show that the O(2')H of Gal has a reduced contact with water due to steric interference caused by the 2-acetamido group of GalNAc. No interaction, in terms of hydrogen bonding exists between the disaccharide and the peptide moieties, but the rotation around the sugar-peptide linkage is restricted. |
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