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. Author manuscript; available in PMC: 2013 May 31.
Published in final edited form as: J Proteomics Bioinform. 2012 May 31;5:127–134. doi: 10.4172/jpb.1000224

Figure 4.

Figure 4

(a) CID MS/MS spectrum of the glycopeptide at m/z 1026.7 (sequence ESVRGNRSLF). Glycosidic bond cleavages were observed, resulting in b,y type ions. The low mass range was dominated by oxonium ions at m/z 366, 528 and 657. The high mass range was dominated by glycopeptides with partial glycan loss and was used to infer glycan composition. (b) ETD MS/MS spectrum of the same glycopeptide. c,z type ions were observed with the intact glycan structure. Peptide sequence and glycosylation site information were obtained from this spectra.