title: Glycoproteins: glycan presentation and protein-fold stability.
abstract: Glycosylation of proteins has been shown to play a role in a variety of cellular events. Thanks to recent advances in obtaining conformational constraints across glycosidic linkages, structural characterisation of glycoproteins has improved considerably. It is now becoming apparent that N-glycosylation of a folded protein can have a significant stabilising effect on large regions of the backbone structure.
authors.affiliation: Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, UK. mark@glycob.ox.ac.uk
authors.forename: M R
authors.initials: MR
authors.lastname: Wormald
authors.forename: R A
authors.initials: RA
authors.lastname: Dwek
mesh_terms: D000818:Animals; D006023:Glycoproteins / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D011134:Polysaccharides / Q000737:chemistry*; D017510:Protein Folding
chemical_list: D006023:Glycoproteins; D011134:Polysaccharides