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dc.contributor.authorTaşoğlu, Çağdaş
dc.contributor.authorGörgülü, Güvenç
dc.contributor.authorYalçın, Talat
dc.date.accessioned2017-04-10T07:47:07Z
dc.date.available2017-04-10T07:47:07Z
dc.date.issued2012-04
dc.identifier.citationTaşoğlu, Ç., Görgülü, G. and Yalçın, T. (2012). Investigation of peptide size, residue position, neighbor amino acid and side chain effect on macrocyclization of b n (n = 5-7) ions. International Journal of Mass Spectrometry, 316-318, 108-116. doi:10.1016/j.ijms.2012.02.001en_US
dc.identifier.issn1387-3806
dc.identifier.urihttp://dx.doi.org/10.1016/j.ijms.2012.02.001
dc.identifier.urihttp://hdl.handle.net/11147/5265
dc.description.abstractA systematic study was carried out to examine the effects of the side chain, peptide size, residue position, and neighboring amino acid on the macrocyclization of b ions. The work utilized isomeric model peptides YAGFLV-NH 2, AGFLVY-NH 2, GFLVYA-NH 2, FLVYAG-NH 2, LVYAGF-NH 2, VYAGFL-NH 2, which all have the same amino acid sequence in cyclic form. The b 6 ions derived from all these isomeric peptides form the same macrocyclic structure due to the generation of the same amino acid sequence order upon cyclization. Hence, the MS/MS spectra and breakdown graphs of b 6 ions derived from these peptides are similar to each other. However, the relative intensities of the non-direct sequence ions in both the MS/MS spectra and breakdown graphs of the b 6 ions derived from FAYVGL-NH 2, GVYALF-NH 2 and VFYLAG-NH 2 show a different distribution from each other and the first series, even though they are all isomeric peptides. This could be due to the different amino acid sequence order in the cyclic forms of these peptides. It is clearly shown that the neighboring amino acid influences the selective opening of the macrocyclic form. Additionally, XYAGFLV-NH 2 and YAGXFLV-NH 2 (where X = C, D, E, H, K, M, N, P, Q, S, T, and W are amino acid residues) were also studied in order to examine the influence of the peptide size, amino acid side chain, and position on the ring formation and cleavage of macrocyclic b 5, b 6 and b 7 ions. The results have clearly shown that b 6 and b 7 ions have a higher tendency of macrocyclization compared to b 5 ions with the exception of QYAGFLV-NH 2. Additionally, it was observed that selective ring opening is also dependent on the size of the b ions and the position of the amino acid residue. From our study of the macrocyclic b 6 ions of our model peptides, the Q, W, K, and M residues were found to be more favorable eliminations when compared to C, D, E, H, N, P, S, and T. Based on the results, no preferential cleavage order can be specified depending on the nature of amino acid side chain.en_US
dc.description.sponsorshipTUBITAK (109T430); DPT (2008K120730); Mass Spectrometry Facilityen_US
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.isversionof10.1016/j.ijms.2012.02.001en_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAmino acid positionen_US
dc.subjectAmino acid side chainen_US
dc.subjectMacrocyclizationen_US
dc.subjectNeighbor amino aciden_US
dc.subjectPeptide sizeen_US
dc.subjectPreferential openingen_US
dc.titleInvestigation of peptide size, residue position, neighbor amino acid and side chain effect on macrocyclization of b n (n = 5-7) ionsen_US
dc.typearticleen_US
dc.contributor.authorIDTR130617en_US
dc.contributor.institutionauthorTaşoğlu, Çağdaş
dc.contributor.institutionauthorGörgülü, Güvenç
dc.contributor.institutionauthorYalçın, Talat
dc.relation.journalInternational Journal of Mass Spectrometryen_US
dc.contributor.departmentİYTE, Fen Fakültesi, Kimya Bölümüen_US
dc.identifier.volume316-318en_US
dc.identifier.startpage108en_US
dc.identifier.endpage116en_US
dc.identifier.wosWOS:000304507000016
dc.identifier.scopusSCOPUS.2-s2.0-84860513753
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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