Physicochemical Characterization of the Reassembled Dimer of an Integral Membrane Protein OmpF Porin |
| |
Authors: | Email author" target="_blank">Yasushi?WatanabeEmail author Yoji?Inoko |
| |
Institution: | (1) National Food Research Institute, 2-1-12 Kannondai, Tsukuba Ibaraki, 305-8642, Japan;(2) Graduate School of Engineering, ScienceOsaka University, 1-3 Machikaneyama, 565-8531 Toyonaka, Osaka, Japan |
| |
Abstract: | The in vitro reassembled species of OmpF porin, which was renatured from its denatured monomer using n-octyl-β-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 β-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. |
| |
Keywords: | CD light scattering membrane protein reassembly SAXS |
本文献已被 PubMed SpringerLink 等数据库收录! |
|