title: One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
abstract: One- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy (at 11.7 Tesla) was used to gain some structural and spectral information about glycophorin AM, glycophorin AM tryptic glycopeptide, a related pentapeptide, and two related monoglycosylated pentapeptides. The protein spectral information suggests that the highly glycosylated N-terminus of glycophorin does not seem to possess a unique tertiary structure. Furthermore, the spectral information provided by the carbohydrate residues also indicates that there is no strong carbohydrate-protein interaction resulting in a unique tertiary structure. This result does not preclude any unique protein-carbohydrate interactions. For the small monoglycosylated pentapeptide containing alpha-D-GalNAc attached to Thr, a unique NOESY cross-peak was observed between the anomeric proton and the beta-proton of Thr. A cross-peak between the beta-proton of Ser and the anomeric proton was not observed for a related monoglycosylated pentapeptide containing alpha-D-GalNAc O-linked to Ser.
authors.affiliation: Department of Chemistry, Clemson University, South Carolina 29634-1905.
authors.forename: K
authors.initials: K
authors.lastname: Dill
authors.forename: S H
authors.initials: SH
authors.lastname: Hu
authors.forename: E
authors.initials: E
authors.lastname: Berman
authors.forename: A A
authors.initials: AA
authors.lastname: Pavia
authors.forename: J M
authors.initials: JM
authors.lastname: Lacombe
mesh_terms: D000818:Animals; D002240:Carbohydrate Sequence; D002247:Carbon Isotopes; D006020:Glycopeptides; D006021:Glycophorins; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D011817:Rabbits; D012795:Sialoglycoproteins; D013057:Spectrum Analysis / Q000379:methods
chemical_list: D002247:Carbon Isotopes; D006020:Glycopeptides; D006021:Glycophorins; D012795:Sialoglycoproteins