(1)H NMR studies of hydroxy protons of the V[beta-Gal(1-->3)-alpha-GalNAc(1-->O)]THPGY glycopeptide.
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.
Kindahl
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L
Department of Chemistry, Swedish University of Agricultural Sciences, PO Box 7015, SE 750 07 Uppsala, Sweden.
Sandström
C
C
Norberg
T
T
Kenne
L
L
D004187:Disaccharides / Q000737:chemistry; D005353:Fibronectins / Q000737:chemistry; D006020:Glycopeptides / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D010446:Peptide Fragments / Q000737:chemistry; D011522:Protons; D013696:Temperature; D014867:Water / Q000737:chemistry
D004187:Disaccharides; D005353:Fibronectins; D006020:Glycopeptides; D010446:Peptide Fragments; D011522:Protons; D014867:Water; C076289:Val(galactosyl-3-galactosyl-N-acetyl)Thr-His-Pro-Gly-Tyr