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.
Highlights
Reviewed by: Cécile Albenne, Université Toulouse III - Paul Sabatier, France Friedrich Altmann, University of Natural Resources and Life Sciences, Austria
The identification, characterization and quantification of post-translational modifications (PTMs) in proteins are a major challenge in the field of proteomics (Heazlewood, 2011)
The examination of protein glycosylation is further complicated by the variations in the glycan structure that can occur on a given polypeptide (Rudd and Dwek, 1997)
Summary
Reviewed by: Cécile Albenne, Université Toulouse III - Paul Sabatier, France Friedrich Altmann, University of Natural Resources and Life Sciences, Austria. Bacic A (2015) Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques.
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