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Peculiarities of thermal denaturation of OmpF porin from Yersinia ruckeri

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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.

Graphical abstract: Peculiarities of thermal denaturation of OmpF porin from Yersinia ruckeri

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Publication details

The article was received on 21 Apr 2017, accepted on 29 Jun 2017 and first published on 20 Jul 2017


Article type: Paper
DOI: 10.1039/C7MB00239D
Citation: Mol. BioSyst., 2017, Advance Article
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    Peculiarities of thermal denaturation of OmpF porin from Yersinia ruckeri

    O. D. Novikova, D. K. Chistyulin, V. A. Khomenko, E. V. Sidorin, N. Yu. Kim, N. M. Sanina, O. Yu. Portnyagina, T. F. Solov'eva, V. N. Uversky and V. L. Shnyrov, Mol. BioSyst., 2017, Advance Article , DOI: 10.1039/C7MB00239D

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