title: Effect of beta-O-glucosylation on L-Ser and L-Thr diamides: a bias toward alpha-helical conformations.
abstract: Beta-D-O-glucosylation produces a remarkable effect on the peptide backbone of the model peptides derived from serine and threonine. Consequently, this type of glycosylation is responsible for the experimentally observed shift from extended conformations (model peptides) towards the folded conformations (model glycopeptides). The conclusion has been solidly assessed by a combined NMR/MD protocol. Interestingly, the MD (molecular dynamics) results for the glycopeptides point towards the existence of water-bridging molecules between the sugar and peptide moieties, which could explain the stabilization of the folded conformers in aqueous solution.
authors.affiliation: Departamento de Química, Universidad de La Rioja UA-CSIC. 26006 Logroño, Spain.
authors.forename: Francisco
authors.initials: F
authors.lastname: Corzana
authors.forename: Jesús H
authors.initials: JH
authors.lastname: Busto
authors.forename: Søren B
authors.initials: SB
authors.lastname: Engelsen
authors.forename: Jesús
authors.initials: J
authors.lastname: Jiménez-Barbero
authors.forename: Juan L
authors.initials: JL
authors.lastname: Asensio
authors.forename: Jesús M
authors.initials: JM
authors.lastname: Peregrina
authors.forename: A
authors.initials: A
authors.lastname: Avenoza
mesh_terms: D002236:Carbohydrate Conformation; D003958:Diamide / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D005947:Glucose / Q000378:metabolism*; D006020:Glycopeptides / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012694:Serine / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics; D013912:Threonine / Q000737:chemistry* / Q000378:metabolism
chemical_list: D006020:Glycopeptides; D003958:Diamide; D013912:Threonine; D012694:Serine; D005947:Glucose