PMID:16096722

Citation	Watanabe, Y and Inoko, Y (2005) Physicochemical characterization of the reassembled dimer of an integral membrane protein OmpF porin. Protein J. 24:167-74
Abstract	The in vitro reassembled species of OmpF porin, which was renatured from its denatured monomer using n-octyl-beta-D-glucopyranoside, was characterized by low-angle laser light scattering photometry, circular dichroism spectroscopy and synchrotron radiation small-angle X-ray scattering measurements. The light scattering measurement reconfirmed that the reassembled species was the dimer of the protein. Circular dichroism spectra of the reassembled dimer showed a native-like beta-structure. A small-angle X-ray scattering measurement indicated that the size of the reassembled dimer was nearly equal to that of the native trimer under the present experimental conditions. In a thermal denaturation experiment followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the reassembled dimer was less stable than the native trimer.
Links	PubMed Online version:10.1007/s10930-005-7840-7
Keywords	Dimerization; Escherichia coli Proteins/chemistry; Porins/chemistry; Protein Conformation; Protein Renaturation
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