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    Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques

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    22
    15
    Author
    Ford, KL; Zeng, W; Heazlewood, JL; Bacic, A
    Date
    2015-08-28
    Source Title
    Frontiers in Plant Science
    Publisher
    FRONTIERS MEDIA SA
    University of Melbourne Author/s
    Heazlewood, Joshua; Bacic, Anthony; Ford, Kristina; Zeng, Wei
    Affiliation
    School of BioSciences
    Metadata
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    Document Type
    Journal Article
    Citations
    Ford, K. L., Zeng, W., Heazlewood, J. L. & Bacic, A. (2015). Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques. FRONTIERS IN PLANT SCIENCE, 6 (AUG), https://doi.org/10.3389/fpls.2015.00674.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/257710
    DOI
    10.3389/fpls.2015.00674
    Abstract
    The analysis of post-translational modifications (PTMs) by proteomics is regarded as a technically challenging undertaking. While in recent years approaches to examine and quantify protein phosphorylation have greatly improved, the analysis of many protein modifications, such as glycosylation, are still regarded as problematic. Limitations in the standard proteomics workflow, such as use of suboptimal peptide fragmentation methods, can significantly prevent the identification of glycopeptides. The current generation of tandem mass spectrometers has made available a variety of fragmentation options, many of which are becoming standard features on these instruments. We have used three common fragmentation techniques, namely CID, HCD, and ETD, to analyze a glycopeptide and highlight how an integrated fragmentation approach can be used to identify the modified residue and characterize the N-glycan on a peptide.

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