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Article: A comparative study of the collision-induced dissociation and the electron capture dissociation of model peptides using electrospray ionization Fourier-transform mass spectrometry

TitleA comparative study of the collision-induced dissociation and the electron capture dissociation of model peptides using electrospray ionization Fourier-transform mass spectrometry
Authors
KeywordsCollision-induced dissociation
Peptides
Electrospray ionization
Electron capture dissociation
Issue Date2004
Citation
European Journal of Mass Spectrometry, 2004, v. 10, n. 4, p. 449-457 How to Cite?
AbstractTandem mass spectra of several model peptides, including KG 3WG3K, NG3WG3N, RG7R, RG3WG3R, RG3DG3R, RG 3EG3R, RG3FG3R and RG 5WG5R were studied using both sustained off-resonance irradiation collision-induced dissociation (SORI-CID) and electron capture dissociation (ECD) methods. By cross comparing the fragmentation pattern of these peptides using the same dissociation method and the same peptide using different dissociation methods, interesting spectral features that are related to the mechanisms of dissociation under SORI-CID and ECD conditions were extracted. Both dissociation methods were believed to be charge-directed. Due presumably to the stepwise ion activation, peptide ion dissociation under SORI-CID conditions was influenced mainly by "localized" hydrogen bonds. Consistent with previous literature findings, mobility proton models could be used to account for the spectral features observed. Substantial changes in the fragmentation patterns of these peptides were observed by using ECD methods. By postulating that the initial tertiary structures of the peptide ions were retained prior to the electron capture process, the changes in fragmentation pattern could be attributed to the directing effect of the "global" hydrogen-bonding network. From the present results, no special preference was observed for cleavage at the backbone linkages adjacent to tryptophan residue over other inter-residual linkages. The previously reported nine-times cleavage preference at the C-terminal side of the tryptophan residue should, therefore, be attributed to some sequence-specific phenomena.
Persistent Identifierhttp://hdl.handle.net/10722/206281
ISSN
2015 Impact Factor: 1.011
2015 SCImago Journal Rankings: 0.380
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorFung, Yi Man Eva-
dc.contributor.authorDuan, Lifang-
dc.contributor.authorChan, Tak Wah Dominic-
dc.date.accessioned2014-10-22T01:25:33Z-
dc.date.available2014-10-22T01:25:33Z-
dc.date.issued2004-
dc.identifier.citationEuropean Journal of Mass Spectrometry, 2004, v. 10, n. 4, p. 449-457-
dc.identifier.issn1469-0667-
dc.identifier.urihttp://hdl.handle.net/10722/206281-
dc.description.abstractTandem mass spectra of several model peptides, including KG 3WG3K, NG3WG3N, RG7R, RG3WG3R, RG3DG3R, RG 3EG3R, RG3FG3R and RG 5WG5R were studied using both sustained off-resonance irradiation collision-induced dissociation (SORI-CID) and electron capture dissociation (ECD) methods. By cross comparing the fragmentation pattern of these peptides using the same dissociation method and the same peptide using different dissociation methods, interesting spectral features that are related to the mechanisms of dissociation under SORI-CID and ECD conditions were extracted. Both dissociation methods were believed to be charge-directed. Due presumably to the stepwise ion activation, peptide ion dissociation under SORI-CID conditions was influenced mainly by "localized" hydrogen bonds. Consistent with previous literature findings, mobility proton models could be used to account for the spectral features observed. Substantial changes in the fragmentation patterns of these peptides were observed by using ECD methods. By postulating that the initial tertiary structures of the peptide ions were retained prior to the electron capture process, the changes in fragmentation pattern could be attributed to the directing effect of the "global" hydrogen-bonding network. From the present results, no special preference was observed for cleavage at the backbone linkages adjacent to tryptophan residue over other inter-residual linkages. The previously reported nine-times cleavage preference at the C-terminal side of the tryptophan residue should, therefore, be attributed to some sequence-specific phenomena.-
dc.languageeng-
dc.relation.ispartofEuropean Journal of Mass Spectrometry-
dc.subjectCollision-induced dissociation-
dc.subjectPeptides-
dc.subjectElectrospray ionization-
dc.subjectElectron capture dissociation-
dc.titleA comparative study of the collision-induced dissociation and the electron capture dissociation of model peptides using electrospray ionization Fourier-transform mass spectrometry-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1255/ejms.648-
dc.identifier.pmid15302969-
dc.identifier.scopuseid_2-s2.0-4644351215-
dc.identifier.volume10-
dc.identifier.issue4-
dc.identifier.spage449-
dc.identifier.epage457-
dc.identifier.isiWOS:000223825300002-

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