Structural Properties of an Engineered Outer Membrane Protein G Mutant, Ompg-16sl, Investigated With Infrared Spectroscopy

dc.authorid Korkmaz, Filiz/0000-0003-3512-3521
dc.authorid Yilmaz, Irem/0009-0002-9551-329X
dc.authorscopusid 57209255624
dc.authorscopusid 56243078100
dc.authorscopusid 8664101000
dc.authorwosid Korkmaz, Filiz/GOH-1457-2022
dc.authorwosid Yildiz, Özkan/P-9207-2016
dc.contributor.author Yilmaz, Irem
dc.contributor.author Yildiz, Ozkan
dc.contributor.author Korkmaz, Filiz
dc.contributor.other Avionics
dc.contributor.other Physics Group
dc.date.accessioned 2024-07-05T15:40:55Z
dc.date.available 2024-07-05T15:40:55Z
dc.date.issued 2020
dc.department Atılım University en_US
dc.department-temp [Yilmaz, Irem] Middle East Tech Univ, Dept Phys, Ankara, Turkey; [Yildiz, Ozkan] Max Planck Inst Biophys, Dept Struct Biol, Frankfurt, Germany; [Korkmaz, Filiz] Atilim Univ, Biophys Lab, Phys Unit, TR-06836 Ankara, Turkey en_US
dc.description Korkmaz, Filiz/0000-0003-3512-3521; Yilmaz, Irem/0009-0002-9551-329X en_US
dc.description.abstract The structural and functional differences between wild type (WT) outer membrane protein G and its two mutants are investigated with Fourier transform infrared spectroscopy. Both mutants have a long extension to the primary sequence to increase the number of beta-strands from 14 (wild type) to 16 in an attempt to enlarge the pore diameter. The comparison among proteins is made in terms of pH-dependent conformational changes and thermal stability. Results show that all proteins respond to pH change but at different degrees. At acidic environment, all proteins contain the same number of residues participated in beta-sheet structure. However, at neutral pH, the mutants have less ordered structure compared to WT porin. Thermal stability tests show that mutants differ significantly from WT porin at neutral pH. Although the transition temperature is directly proportional with the amount of beta-sheet content, the changes in the pre-transition phase that pave the way to structural breakdown are shown to involve interactions among charged residues by two-dimensional correlation spectroscopy analysis. Results of the analysis show that side chain interactions play an active role under increasing temperature. Both mutants have more unordered secondary structure but they respond to pH change in tertiary structure level. Findings of this study provided deeper insight on the active players in structural stability of the WT porin. Communicated by Ramaswamy H. Sarma en_US
dc.description.sponsorship Scientific and Technological Research Council of Turkey (TUBITAK) [214Z085] en_US
dc.description.sponsorship This work was supported by the Scientific and Technological Research Council of Turkey (TUBITAK) [grant number 214Z085]. en_US
dc.identifier.citationcount 5
dc.identifier.doi 10.1080/07391102.2019.1624617
dc.identifier.endpage 2115 en_US
dc.identifier.issn 0739-1102
dc.identifier.issn 1538-0254
dc.identifier.issue 7 en_US
dc.identifier.pmid 31157607
dc.identifier.scopus 2-s2.0-85067055487
dc.identifier.startpage 2104 en_US
dc.identifier.uri https://doi.org/10.1080/07391102.2019.1624617
dc.identifier.uri https://hdl.handle.net/20.500.14411/3394
dc.identifier.volume 38 en_US
dc.identifier.wos WOS:000472321900001
dc.identifier.wosquality Q1
dc.institutionauthor Yılmaz, İrem
dc.institutionauthor Korkmaz Özkan, Filiz
dc.language.iso en en_US
dc.publisher Taylor & Francis inc en_US
dc.relation.publicationcategory Makale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı en_US
dc.rights info:eu-repo/semantics/closedAccess en_US
dc.scopus.citedbyCount 5
dc.subject OmpG en_US
dc.subject porin en_US
dc.subject infrared spectroscopy en_US
dc.subject protein engineering en_US
dc.subject 2DCOS analysis en_US
dc.title Structural Properties of an Engineered Outer Membrane Protein G Mutant, Ompg-16sl, Investigated With Infrared Spectroscopy en_US
dc.type Article en_US
dc.wos.citedbyCount 5
dspace.entity.type Publication
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