The potency of amide protons for assignments of NMR spectra of carbohydrate chains of glycoproteins, recorded in 1H2O solutions

FEBS Lett. 1991 Aug 5;287(1-2):108-12. doi: 10.1016/0014-5793(91)80027-z.

Abstract

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 now [corrected] become amenable for conformational studies by multidimensional NMR in 1H2O solution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / chemistry
  • Carbohydrate Sequence
  • Carbohydrates / chemistry*
  • Disaccharides*
  • Glucans / chemistry
  • Glycoproteins / chemistry*
  • Magnetic Resonance Spectroscopy*
  • Molecular Sequence Data
  • N-Acetylneuraminic Acid
  • Polysaccharides / chemistry
  • Sialic Acids / chemistry
  • Solutions
  • Water

Substances

  • Carbohydrates
  • Disaccharides
  • Glucans
  • Glycoproteins
  • Polysaccharides
  • Sialic Acids
  • Solutions
  • Water
  • N,N-diacetylchitobiose
  • N-Acetylneuraminic Acid
  • Acetylglucosamine