Application of high-field proton magnetic resonance spectroscopy in the structural determination of membrane-derived Sindbis virus glycopeptides.
Sindbis virus membrane glycopeptides have ben purified in chemical quantities and their oligosaccharide structures analyzed by 1H NMR spectroscopy at 360 MHz. Interpretable spectra could be obtained with approximately 100 micrograms of oligosaccharide. Spectral analysis of the sialyl glycopeptides S1, S2, and S3 at high and low temperatures confirms their structures to be NANA alpha (2,3)Gal beta (1,4)-GlcNAc beta (1,2)Man alpha (1,6)-[NANA alpha (2,3)Gal beta (1,4)-GlcNAc beta (1,2)Man alpha (1,3)]-Man beta (1,4)GlcNAc beta (1,4)-[Fuc alpha-(1,6)]-GlcNAc beta 1-Asn. These are heterogeneous with respect to sialic acid (NANA). Spectra of two endo-beta-N-acetylglucosaminidase products of the S4 glycopeptides are reported. The interpretation of these spectra is consistent with Man5GlcNAc and Man7GlcNAc oligosaccharide structures. Their chemical shifts are essentially identical with those reported for ovalbumin glycopeptides of the same composition, with exception to the perturbations arising from their oligosaccharide nature.
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002642:Chick Embryo; D006020:Glycopeptides; D009682:Magnetic Resonance Spectroscopy; D012845:Sindbis Virus / Q000032:analysis*; D014764:Viral Proteins
D006020:Glycopeptides; D014764:Viral Proteins