<i>In situ</i> opening/closing of OmpG from <i>E</i>. <i>coli</i> and the splitting of β-sheet signals in ATR-FTIR spectroscopy

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dc.authoridKorkmaz, Filiz/0000-0003-3512-3521
dc.authoridYildiz, Ozkan/0000-0003-3659-2805
dc.authorscopusid8664101000
dc.authorscopusid7004541359
dc.authorscopusid56243078100
dc.authorscopusid7006210611
dc.authorwosidKorkmaz, Filiz/GOH-1457-2022
dc.authorwosidMäntele, Werner/IRZ-8754-2023
dc.authorwosidYildiz, Ozkan/P-9207-2016
dc.contributor.authorKorkmaz Özkan, Filiz
dc.contributor.authorKoester, Stefan
dc.contributor.authorYildiz, Oezkan
dc.contributor.authorMaentele, Werner
dc.contributor.otherPhysics Group
dc.date.accessioned2024-07-05T15:11:01Z
dc.date.available2024-07-05T15:11:01Z
dc.date.issued2012
dc.departmentAtılım Universityen_US
dc.department-temp[Korkmaz, Filiz] Atilim Univ, Phys Unit, Biophys Lab, TR-06836 Ankara, Turkey; [Korkmaz, Filiz; Maentele, Werner] Goethe Univ Frankfurt, Inst Biophys, D-60438 Frankfurt, Germany; [Koester, Stefan; Yildiz, Oezkan] Max Planck Inst Biophys, Dept Biol Struct, D-60438 Frankfurt, Germanyen_US
dc.descriptionKorkmaz, Filiz/0000-0003-3512-3521; Yildiz, Ozkan/0000-0003-3659-2805en_US
dc.description.abstractThe pH dependent opening and closure of Escherichia coli OmpG is driven by the formation and breaking of hydrogen bridges in beta-strands S11-S13. We have investigated the in situ secondary structural changes of OmpG with ATR-FTIR difference spectroscopy in order to detect the signals associated with the newly established interactions. Curve-fitting of OmpG in two pH conditions revealed the splitting and shifting of beta-sheet signals upon opening of the channel. Besides secondary structure changes, there are also amino acid side chain signals that play active role in opening/closing of the channel. An interaction among positively charged arginines and negatively charged aspartic and glutamic acid residues is suggested upon closure of the channel while this interaction is abolished when the channel opens at higher pH. (C) 2012 Elsevier B.V. All rights reserved.en_US
dc.description.sponsorship[SFB 472/P21]; [YI 96/3-1]en_US
dc.description.sponsorshipThe authors gratefully acknowledge the financial support from SFB 472/P21 and YI 96/3-1. Dr. Enela Dzafic is also greatly acknowledged for her help in ATR-FTIR spectroscopy.en_US
dc.identifier.citation18
dc.identifier.doi10.1016/j.saa.2012.01.025
dc.identifier.endpage401en_US
dc.identifier.issn1386-1425
dc.identifier.pmid22402479
dc.identifier.scopus2-s2.0-84859095241
dc.identifier.scopusqualityQ1
dc.identifier.startpage395en_US
dc.identifier.urihttps://doi.org/10.1016/j.saa.2012.01.025
dc.identifier.urihttps://hdl.handle.net/20.500.14411/1393
dc.identifier.volume91en_US
dc.identifier.wosWOS:000303073300058
dc.identifier.wosqualityQ1
dc.language.isoenen_US
dc.publisherPergamon-elsevier Science Ltden_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectbeta-Barrel membrane proteinen_US
dc.subjectSecondary structure determinationen_US
dc.subjectFT-IR spectroscopyen_US
dc.subjectAmide-I band analysisen_US
dc.subjectCurve-fittingen_US
dc.subjectDifference spectrumen_US
dc.title<i>In situ</i> opening/closing of OmpG from <i>E</i>. <i>coli</i> and the splitting of β-sheet signals in ATR-FTIR spectroscopyen_US
dc.typeArticleen_US
dspace.entity.typePublication
relation.isAuthorOfPublication1ebbd479-dfc4-411f-8702-e06ba4616da2
relation.isAuthorOfPublication.latestForDiscovery1ebbd479-dfc4-411f-8702-e06ba4616da2
relation.isOrgUnitOfPublication2682824b-512d-4a4e-8498-5b5719f606fe
relation.isOrgUnitOfPublication.latestForDiscovery2682824b-512d-4a4e-8498-5b5719f606fe

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