Peculiarities of Thermal Denaturation of OmpF Porin from Yersinia Ruckeri
Document Type
Article
Publication Date
2017
Digital Object Identifier (DOI)
https://doi.org/10.1039/C7MB00239D
Abstract
Irreversible denaturation of membrane proteins in detergent solutions is similar to unfolding of water-soluble multidomain proteins and represents a complex, multistage process. Pore-forming proteins of Gram-negative bacteria are heat-modifiable proteins, i.e., proteins altering their molecular forms (trimers or monomers), and accordingly, their electrophoretic mobilities depending upon denaturation conditions. There are still some contradictory data on the peculiarities of the conformational changes in the porin structure with temperature. Some authors demonstrated the loss of the porin trimeric structure only after unfolding of monomer subunits. Other researchers initially observed the dissociation of porin oligomers into the folded monomers. Using SDS-PAGE, spectroscopic methods and differential scanning calorimetry, a detailed study of thermally induced changes in the spatial structure of OmpF porin from the fish pathogen Yersinia ruckeri (Yr-OmpF) was carried out. The data obtained allowed us to conclude unambiguously that changes in the spatial structure of the monomers of Yr-OmpF precede the dissociation of the porin trimer.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Molecular BioSystems, v. 13, issue 9, p. 1854-1862
Scholar Commons Citation
Novikova, Olga D.; Chistyulin, Dmitry K.; Khomenko, Valentina A.; Sidorin, Evgeny V.; Kim, Natalya Yu.; Sanina, Nina M.; Portnyagina, Olga Yu.; Solov'eva, Tamara F.; Uversky, Vladimir N.; and Shnyrov, Valery L., "Peculiarities of Thermal Denaturation of OmpF Porin from Yersinia Ruckeri" (2017). Molecular Medicine Faculty Publications. 275.
https://digitalcommons.usf.edu/mme_facpub/275
