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The potency of amide protons for assignments of NMR spectra of carbohydrate chains of glycoproteins, recorded in 1 H 2 O solutions
Author(s) -
Hård Karl,
Spronk Bertina A.,
Hokke Cornelis H.,
Kamerling Johannis P.,
Vliegenthart Johannes F.G.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80027-z
Subject(s) - chemistry , glycan , oligosaccharide , amide , glycoprotein , stereochemistry , nuclear magnetic resonance spectroscopy , sialic acid , carbohydrate conformation , glycopeptide , nmr spectra database , n acetylglucosamine , chemical shift , spectral line , biochemistry , enzyme , physics , astronomy , antibiotics
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 1 H 2 O 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 1 H 2 O solution.