Abstract：
:Glycosylation is one of the most common post-translational modifications in proteins, existing in ~50% of mammalian proteins. Several research groups have demonstrated that mass spectrometry is an efficient technique for glycopeptide identification; however, this problem is still challenging because of the enormous diversity of glycan structures and the microheterogeneity of glycans. In addition, a glycopeptide may contain multiple glycosylation sites, making the problem complex. Current software tools often fail to identify glycopeptides with multiple glycosylation sites, and hence we present GlycoMID, a graph-based spectral alignment algorithm that can identify glycopeptides with multiple hydroxylysine O-glycosylation sites by tandem mass spectra. GlycoMID was tested on mass spectrometry data sets of the bovine collagen α-(II) chain protein, and experimental results showed that it identified more glycopeptide-spectrum matches than other existing tools, including many glycopeptides with two glycosylation sites.
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Zhang Y,Yu CY,Song E,Li SC,Mechref Y,Tang H,Liu Xdoi
10.1021/acs.jproteome.5b00299subject
Has Abstractpub_date
2015-12-04 00:00:00pages
5099-108issue
12eissn
1535-3893issn
1535-3907journal_volume
14pub_type
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