Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5154
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dc.contributor.authorAtik, Ahmet Emin-
dc.contributor.authorYalçın, Talat-
dc.date.accessioned2017-03-28T08:20:38Z
dc.date.available2017-03-28T08:20:38Z
dc.date.issued2013-10
dc.identifier.citationAtik, A.E., and Yalçın, T. (2013). Protonated dipeptide losses from b 5 and b 4 ions of side chain hydroxyl group containing pentapeptides. Journal of the American Society for Mass Spectrometry, 24(10). 1543-1554. doi:10.1007/s13361-013-0694-xen_US
dc.identifier.issn1044-0305
dc.identifier.issn1044-0305-
dc.identifier.issn1879-1123-
dc.identifier.urihttps://doi.org/10.1007/s13361-013-0694-x
dc.identifier.urihttp://hdl.handle.net/11147/5154
dc.description.abstractIn this study, C-terminal protonated dipeptide eliminations were reported for both b 5 and b 4 ions of side chain hydroxyl group (-OH) containing pentapeptides. The study utilized the model C-terminal amidated pentapeptides having sequences of XGGFL and AXVYI, where X represents serine (S), threonine (T), glutamic acid (E), aspartic acid (D), or tyrosine (Y) residue. Upon low-energy collision-induced dissociation (CID) of XGGFL (where X = S, T, E, D, and Y) model peptide series, the ions at m/z 279 and 223 were observed as common fragments in all b 5 and b 4 ion (except b 4 ion of YGGFL) mass spectra, respectively. By contrast, peptides, namely SMeGGFL-NH2 and EOMeGGFL- NH2, did not show either the ion at m/z 279 or the ion at m/z 223. It is shown that the side chain hydroxyl group is required for the possible mechanism to take place that furnishes the protonated dipeptide loss from b 5 and b 4 ions. In addition, the ions at m/z 295 and 281 were detected as common fragments in all b 5 and b 4 ion (except b 4 ion of AYVYI) mass spectra, respectively, for AXVYI model peptide series. The MS4 experiments exhibited that the fragment ions at m/z 279, 223, 295, and 281 entirely reflect the same fragmentation behavior of [M + H]+ ion generated from commercial dipeptides FL-OH, GF-OH, YI-OH, and VY-OH. These novel eliminations reported here for b 5 and b 4 ions can be useful in assigning the correct and reliable peptide sequences for high-throughput proteomic studies. [Figure not available: see fulltext.]en_US
dc.description.sponsorshipScientific and Technological Research Council of Turkey (109T430); State Planning Organization (Turkey)en_US
dc.language.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofJournal of the American Society for Mass Spectrometryen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectDipeptide lossen_US
dc.subjectMacrocyclizationen_US
dc.subjectPeptide fragmentationen_US
dc.subjectWater migrationen_US
dc.subjectIonsen_US
dc.titleProtonated dipeptide losses from b 5 and b 4 ions of side chain hydroxyl group containing pentapeptidesen_US
dc.typeArticleen_US
dc.authoridTR130617en_US
dc.institutionauthorAtik, Ahmet Emin-
dc.institutionauthorYalçın, Talat-
dc.departmentİzmir Institute of Technology. Chemistryen_US
dc.identifier.volume24en_US
dc.identifier.issue10en_US
dc.identifier.startpage1543en_US
dc.identifier.endpage1554en_US
dc.identifier.wosWOS:000324234300011en_US
dc.identifier.scopus2-s2.0-84884555901en_US
dc.relation.tubitakinfo:eu-repo/grantAgreement/TUBITAK/TBAG/109T430en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1007/s13361-013-0694-x-
dc.identifier.pmid23900715en_US
dc.relation.doi10.1007/s13361-013-0694-xen_US
dc.coverage.doi10.1007/s13361-013-0694-xen_US
dc.identifier.wosqualityQ1-
dc.identifier.scopusqualityQ1-
item.openairetypeArticle-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextopen-
item.fulltextWith Fulltext-
item.languageiso639-1en-
item.cerifentitytypePublications-
crisitem.author.dept04.01. Department of Chemistry-
Appears in Collections:Chemistry / Kimya
PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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