Investigations of Ph-Dependent Dynamic Properties of Ompg-16sl, an Outer Membrane Protein G Mutant by Atr-Ftir Spectroscopy

dc.authorid Korkmaz, Filiz/0000-0003-3512-3521
dc.authorid Yilmaz, Irem/0009-0002-9551-329X
dc.authorscopusid 57209255624
dc.authorscopusid 8664101000
dc.authorwosid Korkmaz, Filiz/GOH-1457-2022
dc.contributor.author Yilmaz, Irem
dc.contributor.author Korkmaz, Filiz
dc.contributor.other Avionics
dc.contributor.other Physics Group
dc.date.accessioned 2024-07-05T15:17:42Z
dc.date.available 2024-07-05T15:17:42Z
dc.date.issued 2022
dc.department Atılım University en_US
dc.department-temp [Yilmaz, Irem; Korkmaz, Filiz] Atilim Univ, Phys Unit, Biophys Lab, 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 In this paper, the dynamic properties of outer membrane protein G mutant (OmpG-16SL) are investigated with ATR-FTIR spectroscopy. While OmpG-WT has 14 beta-strands in its structure, the mutant is designed to have 16 beta-strands with the intention of creating an enlarged pore. Loop L6 is elongated by introducing six residues, two of which are negatively charged. The solvent accessibility of the OmpG-16SL mutant is compared with WT and a previously reported mutant OmpG-16S by tracking the H-1/H-2 exchange kinetics in acidic and neutral buffer conditions. The exchange kinetics and dynamics in the fast and slow exchange phases are separately investigated using the 2DCOS technique, which enables the tracking of the structural changes at each phase of the exchange process. The results suggest that the mutant OmpG-16SL is equally exposed to buffer in both acidic and neutral pH conditions. Additionally, the time range in the fast phase is very short - one-tenth of that for WT - and most of the exchange is completed in this phase. This fast exchange within minutes is also indicative of the presence of highly flexible and/or unstructured regions. In all, the fast exchange rates independent of the buffer pH justify the assumption that there is an altered interaction among the charged residues, which leads to a steadily-open pore. The role of the side-chain interactions within the pore and between the loops involving the loop L6 is also discussed. 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 2
dc.identifier.doi 10.1016/j.bbapap.2022.140780
dc.identifier.issn 1570-9639
dc.identifier.issn 1878-1454
dc.identifier.issue 5 en_US
dc.identifier.pmid 35405324
dc.identifier.scopus 2-s2.0-85128244133
dc.identifier.scopusquality Q2
dc.identifier.uri https://doi.org/10.1016/j.bbapap.2022.140780
dc.identifier.uri https://hdl.handle.net/20.500.14411/1774
dc.identifier.volume 1870 en_US
dc.identifier.wos WOS:000821941900001
dc.identifier.wosquality Q2
dc.institutionauthor Yılmaz, İrem
dc.institutionauthor Korkmaz Özkan, Filiz
dc.language.iso en en_US
dc.publisher Elsevier 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 2
dc.subject OmpG en_US
dc.subject ATR-FTIR spectroscopy en_US
dc.subject 2D correlation spectroscopy en_US
dc.subject pH-gating en_US
dc.subject Quiet pore en_US
dc.title Investigations of Ph-Dependent Dynamic Properties of Ompg-16sl, an Outer Membrane Protein G Mutant by Atr-Ftir Spectroscopy en_US
dc.type Article en_US
dc.wos.citedbyCount 2
dspace.entity.type Publication
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