Zhang, YanlinYu, Chuan-YihSong, EhwangLi, Shuai ChengMechref, YehiaTang, HaixuLiu, Xiaowen2016-08-162016-08-162015-11Zhang, Y., Yu, C.-Y., Song, E., Li, S. C., Mechref, Y., Tang, H., & Liu, X. (2015). Identification of Glycopeptides with Multiple Hydroxylysine O-Glycosylation Sites by Tandem Mass Spectrometry. Journal of Proteome Research, 14(12), 5099–5108. http://doi.org/10.1021/acs.jproteome.5b00299https://hdl.handle.net/1805/10701Glycosylation 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.enPublisher Policyalignment algorithmcollagen α-(II) chainglycopeptide identificationArticle