Circular dichroism studies of synthetic Asn-X-Ser/Thr-containing peptides: Structure-glycosylation relationship

作者: J.P. Aubert , N. Helbecque , M.H. Loucheux-Lefebvre

DOI: 10.1016/0003-9861(81)90118-1

关键词: TripeptideProtein secondary structureOligosaccharidePeptideBiochemistryCircular dichroismChemistryGlycosylStereochemistryGlycoproteinGlycosylationBiophysicsMolecular biology

摘要: Abstract Many proteins are glycosylated and widely distributed. Knowledge of the biosynthetic pathway is great interest in elucidating exact role oligosaccharide chain glycoproteins. It now possible to glycosylate carbohydrate-depleted or chemically denatured glycoproteins synthetic Asn-X-Thr/Ser-containing peptides a cell-free system. The results obtained showed that it tripeptide but yield (of glycosylation) increases as length peptide increases. We have shown native glycoproteins, chains always situated β-turn. seemed so very interesting see if this condition was necessary for glycosylation. To elucidate problem, were tested glycosyl acceptors using hen oviduct membranes enzyme source. These studied by circular dichroism aqueous lipid mixtures presence secondary structure state promotes greatly

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