One- and two-dimensional NMR studies of the N-terminal portion of glycophorin A at 11.7 Tesla.
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.
Dill
K
K
Department of Chemistry, Clemson University, South Carolina 29634-1905.
Hu
S H
SH
Berman
E
E
Pavia
A A
AA
Lacombe
J M
JM
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
D002247:Carbon Isotopes; D006020:Glycopeptides; D006021:Glycophorins; D012795:Sialoglycoproteins