title: Conformation of glycopeptides.
abstract: The presence of carbohydrate side-chains in native glycoproteins alters a number of biochemical properties of the peptide backbone. One of the most frequently studied questions is the conformation-modifying effect of sugar incorporation into asparagine, serine and threonine residues. When N-glycosylation modifies the conformation, the resulting structures are more ordered than the peptide chain without sugar addition. For O-glycopeptides the final conformations can be either more ordered or less ordered. In any event, only the innermost carbohydrates make contact with the peptide backbone. Through-space structural changes are mostly found downstream of the O-glycosylation site. In the repeat unit of epithelial mucin-1 protein, clustering of the carbohydrates results in an easily observable stabilization of the poly-proline II helix.
authors.affiliation: The Wistar Institute, Philadelphia, Pennsylvania 19104, USA. Otvos@wistar.upenn.edu
authors.forename: Laszlo
authors.initials: L
authors.lastname: Otvos
authors.forename: Mare
authors.initials: M
authors.lastname: Cudic
mesh_terms: D019295:Computational Biology; D006020:Glycopeptides / Q000737:chemistry*; D006031:Glycosylation; D008968:Molecular Conformation; D009077:Mucins / Q000096:biosynthesis / Q000737:chemistry
chemical_list: D006020:Glycopeptides; D009077:Mucins