Characterization of heat-treatment properties of a membrane protein solubilized in the presence of a surfactant
2016
Watanabe, Y. (NARO, National Food Research Institute, Tsukuba, Ibaraki (Japan))
In order to understand the structural properties of a food-related hydrophobic protein, the heat-induced denaturation of an integral membrane protein OmpF porin in the presence of an anionic surfactant, sodium dodecyl sulfate, was characterized by circular dichroism spectroscopy and gel electrophoresis. The cooperative irreversible transition of the mean residue ellipticity of OmpF porin was observed between 60 degC and 80 degC at pH 7. The native beta-structure of OmpF porin trimer is converted to an alpha-helix-like structure of the denatured monomer upon heating. The denatured protein in the presence of sodium dodecyl sulfate has no transition upon heating as followed by circular dichroism spectroscopy. This property will be the same as that of protein polypeptides derived from water-soluble proteins in complex with the surfactant micelles.
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