Characterization of the molecular assembly of a membrane protein in solution
2009
Watanabe, Y.(National Food Research Inst., Tsukuba, Ibaraki (Japan)) | Inoko, Y.
The molecular assembly of an integral membrane protein porin in the presence of a non-ionic surfactant, octyl glucoside, was characterized by using synchrotron radiation solution X-ray scattering measurements. The membrane protein was solubilized as a trimeric form at 7 and 6 mg/ml octyl glucoside (at and just below its critical micelle concentration). The higher order aggregates of the protein were observed at 5.4 mg/ml octyl glucoside. The scattering pattern suggests that the assembly of the aggregates was made in the plane direction.
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