Search

Three glycoprotein N-glycans, namely, a disialylated diantennary carbohydrate chain linked to Asn. a monosialylated, fucosylated diantennary glycopeptide with bisecting N-acetylglucosamine, and a tetrasialylated, fucosylated tetra-antennary oligosaccharide. have been investigated by two-dimensional NOE and HOHAHA spectroscopy in 1H 2O as solvent. The amide protons of all N-acetylglucosamine and sialic acid residues could readily be assigned. The large chemical-shift dispersion of the amide resonances of the N-acetylglucosamine residues, allowed the unambiguous assignment of every N-acetyl methyl signal, via strong NOEs. Subspectra could be obtained of all N-acetylglucosamine residues in HOHAHA spectra. These results have as main implication that several biologically important large glycans, will not become amenable for conformational studies by multidimensional NMR in 1H 2O solution.

Three glycoprotein N‐glycans, namely, a disialylated diantennary carbohydrate chain linked to Asn. a monosialylated, fucosylated diantennary glycopeptide with bisecting N‐acetylglucosamine, and a tetrasialylated, fucosylated tetra‐antennary oligosaccharide. have been investigated by two‐dimensional NOE and HOHAHA spectroscopy in 1H2O as solvent. The amide protons of all N‐acetylglucosamine and sialic acid residues could readily be assigned. The large chemical‐shift dispersion of the amide resonances of the N‐acetylglucosamine residues, allowed the unambiguous assignment of every N‐acetyl methyl signal, via strong NOEs. Subspectra could be obtained of all N‐acetylglucosamine residues in HOHAHA spectra. These results have as main implication that several biologically important large glycans, will not become amenable for conformational studies by multidimensional NMR in 1H2O solution.