Possible role of the carbohydrate residues on the structure of the N-terminus of glycophorin AM.
Natural-abundance 13C nuclear magnetic resonance (13C-n.m.r.) was used to study the effect of monoglycosylation on the structure and dynamics of a pentapeptide related to the N-terminus of glycophorin AM. The results of this study indicate that a single point of glycosylation, on the pentapeptide, can significantly affect its structure. Moreover, glycosylation of this pentapeptide also affects its dynamic motion in solution. This study further defines the role that the carbohydrate residue plays in determining the structure about the N-terminus of glycophorin AM.
D002240:Carbohydrate Sequence; D006020:Glycopeptides; D006021:Glycophorins; D006863:Hydrogen-Ion Concentration; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides / Q000138:chemical synthesis*; D012795:Sialoglycoproteins
D006020:Glycopeptides; D006021:Glycophorins; D007202:Indicators and Reagents; D009842:Oligopeptides; D012795:Sialoglycoproteins