4.2 Review

Intact glycopeptide characterization using mass spectrometry

Journal

EXPERT REVIEW OF PROTEOMICS
Volume 13, Issue 5, Pages 513-522

Publisher

TAYLOR & FRANCIS LTD
DOI: 10.1586/14789450.2016.1172965

Keywords

Glycosylation; glycopeptide; post-translational modification; LC-MS; MS; proteomics; bioinformatics

Funding

  1. OU startup funds
  2. NIH [5U01AI101990-04 BRI, FY15109843]
  3. EMSL intramural research projects
  4. EMSL capability development projects

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Glycosylation is one of the most prominent and extensively studied protein post-translational modifications. However, traditional proteomic studies at the peptide level (bottom-up) rarely characterize intact glycopeptides (glycosylated peptides without removing glycans), so no glycoprotein heterogeneity information is retained. Intact glycopeptide characterization, on the other hand, provides opportunities to simultaneously elucidate the glycan structure and the glycosylation site needed to reveal the actual biological function of protein glycosylation. Recently, significant improvements have been made in the characterization of intact glycopeptides, ranging from enrichment and separation, mass spectroscopy (MS) detection, to bioinformatics analysis. In this review, we recapitulated currently available intact glycopeptide characterization methods with respect to their advantages and limitations as well as their potential applications.

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