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Glycomics is a subset of the field of glycobiology that aims to identify the structure and function of the complete set of glycans (the glycome) produced in a given cell or organism and identify all the genes that encode glycoproteins.
Protein glycosylation is a heterogeneous post-translational modification that generates greater proteomic diversity that is difficult to analyze. Here the authors describe pGlyco 2.0, a workflow for the precise one step identification of intact N-glycopeptides at the proteome scale.
An inactive mutant of a bacterial O-GlcNAc hydrolase was used as an affinity reagent to enrich O-GlcNAc-modified proteins from Drosophila embryos and led to the identification, by MS–proteomics, of O-GlcNAcylated proteins involved in embryogenesis.
The comprehensive study of protein glycosylation has been complicated by the complex structural diversity of glycans. In this protocol, Yang et al. describe a solid-phase method for the sequential analysis of N-linked and O-linked glycans.