Please use this identifier to cite or link to this item: https://hdl.handle.net/11147/5266
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dc.contributor.authorAtik, Ahmet Emin-
dc.contributor.authorGörgülü, Güvenç-
dc.contributor.authorYalçın, Talat-
dc.date.accessioned2017-04-10T07:55:35Z-
dc.date.available2017-04-10T07:55:35Z-
dc.date.issued2012-04-
dc.identifier.citationAtik, A. E., Görgülü, G. and Yalçın, T. (2012). The role of lysine ε-amine group on the macrocyclization of b ions. International Journal of Mass Spectrometry, 316-318, 84-90. doi:10.1016/j.ijms.2011.12.008en_US
dc.identifier.issn1387-3806-
dc.identifier.urihttp://dx.doi.org/10.1016/j.ijms.2011.12.008-
dc.identifier.urihttp://hdl.handle.net/11147/5266-
dc.description.abstractA study was carried out to examine if the amine (NH 2) group located on the side chains of lysine (K), glutamine (Q), or asparagine (N) residue has any effect on the macrocyclization of b ions even though the N-terminals of the peptides were acetylated. The work utilized the model peptides Ac-KYAGFLVG, Ac-QYAGFLV-NH 2, and Ac-NYAGFLV-NH 2. The CID mass spectra of b 7 ions originated from these three peptides exhibited that the macrocyclization still occurred for the lysine containing peptide in spite of the N-terminal of the peptide was acetylated, but was failed to be observed for glutamine and asparagine containing peptides. These current results reveal that the lysine side chain ε-amine group has been involved in the macrocyclization of the peptide b ions for the N-terminal acetylated peptides and consequently, non-direct sequence b ions were observed in the CID mass spectra. However, due to the amide group on the side chains of the glutamine and asparagine residues, the nucleophilicity of their groups greatly reduced; therefore the scrambling b ions were not detected in their b 7 ion CID mass spectra. In addition, the effect of the lysine position was also studied for series of six isomeric octapeptides such as, Ac-KYAGFLVG, Ac-YKAGFLVG, Ac-YAKGFLVG, Ac-YAGKFLVG, Ac-YAGFKLVG and Ac-YAGFLKVG in order to examine the relationship between the intensities of non-direct sequence b ions and the lysine position in the octapeptide series. The results clearly demonstrated that the most abundant non-direct sequence b ions were observed for the first position of lysine residue in the N-terminal acetylated octapeptide, however, when the lysine residue gets closer to the C-terminal position the relative intensities of the scrambled b ions were greatly decreased.en_US
dc.description.sponsorshipTUBITAK (109T430); Mass Spectrometry Facilityen_US
dc.language.isoenen_US
dc.publisherElsevier Ltd.en_US
dc.relation.ispartofInternational Journal of Mass Spectrometryen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAsparagineen_US
dc.subjectGlutamineen_US
dc.subjectLysine side chain ε-amine groupen_US
dc.subjectMacrocyclization of b ionsen_US
dc.subjectN-terminal acetylationen_US
dc.titleThe role of lysine ?-amine group on the macrocyclization of b ionsen_US
dc.typeArticleen_US
dc.authoridTR130617en_US
dc.institutionauthorAtik, Ahmet Emin-
dc.institutionauthorGörgülü, Güvenç-
dc.institutionauthorYalçın, Talat-
dc.departmentİzmir Institute of Technology. Chemistryen_US
dc.identifier.volume316-318en_US
dc.identifier.startpage84en_US
dc.identifier.endpage90en_US
dc.identifier.wosWOS:000304507000013en_US
dc.identifier.scopus2-s2.0-84860522272en_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.identifier.doi10.1016/j.ijms.2011.12.008-
dc.relation.doi10.1016/j.ijms.2011.12.008en_US
dc.coverage.doi10.1016/j.ijms.2011.12.008en_US
dc.identifier.wosqualityQ2-
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
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection
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