A two-dimensional 1H-n.m.r. (500 MHz) and 13C-n.m.r. (125 MHz) study of N-linked glycopeptides derived from calf fetuin.
The oligosaccharide part of an N-linked triantennary glycopeptide from calf fetuin with fourteen carbohydrate residues and its smaller derivatives obtained by successive enzymic cleavage of the terminal residues were investigated using 2D 1H-n.m.r. (500 MHz) and 13C-n.m.r. (125 MHz) spectroscopy. Assignments have been made of the resonances of almost all the protons of the constituent carbohydrate residues in these glycopeptides. A comparison of the 1H chemical shifts and coupling constants, as determined from the cross-peaks, has shown the dependence of these parameters on the interactions of spatially related neighbouring carbohydrates. Small conformational changes take place upon elongation of the oligosaccharide side-chains.
Berman
E
E
Max-Planck-Institut für Medizinische Forschung, Heidelberg, F.R.G.
Dabrowski
U
U
Dabrowski
J
J
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002247:Carbon Isotopes; D006020:Glycopeptides; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D000509:alpha-Fetoproteins
D002247:Carbon Isotopes; D006020:Glycopeptides; D000509:alpha-Fetoproteins; D006859:Hydrogen