Yılmaz, İremYilmaz, IremKorkmaz, FilizKorkmaz Özkan, FilizAvionicsPhysics Group2024-07-052024-07-05202221570-96391878-145410.1016/j.bbapap.2022.1407802-s2.0-85128244133https://doi.org/10.1016/j.bbapap.2022.140780https://hdl.handle.net/20.500.14411/1774Korkmaz, Filiz/0000-0003-3512-3521; Yilmaz, Irem/0009-0002-9551-329XIn 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.eninfo:eu-repo/semantics/closedAccessOmpGATR-FTIR spectroscopy2D correlation spectroscopypH-gatingQuiet poreArticleQ2Q218705WOS:00082194190000135405324