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• W2103750034 abstract "Collision-induced dissociation (CID) tandem mass spectrometry (MS/MS) does not allow the characterization of glycopeptides because of the fragmentation of glycan structures and limited fragmentation of peptide backbones. Electron transfer dissociation (ETD) MS/MS, on the other hand, offers a complementary approach, prompting only peptide backbone fragmentation while keeping post-translational modifications intact. Characterization of glycopeptides using both CID and ETD is summarized in this unit. While CID provides information related to the composition of glycan moieties attached to a peptide backbone, ETD permits de novo sequencing of peptides. Radical anion transfer of electrons to the peptide backbone in ETD induces cleavage of the N-Cα bond. The glycan moiety is retained on the peptide backbone, largely unaffected by the ETD process, thus allowing the identification of the amino acid sequence of a glycopeptide and its glycosylation site. This unit discusses the use of both CID and ETD for better characterization of glycopeptides. Curr. Protoc. Protein Sci. 68:12.11.1-12.11.11. © 2012 by John Wiley & Sons, Inc." @default.
• W2103750034 created "2016-06-24" @default.
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• W2103750034 date "2012-04-01" @default.
• W2103750034 modified "2023-10-16" @default.
• W2103750034 title "Use of CID/ETD Mass Spectrometry to Analyze Glycopeptides" @default.
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• W2103750034 doi "https://doi.org/10.1002/0471140864.ps1211s68" @default.
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