Effect of various mild surfactants on the reassembly of an oligomeric integral membrane protein OmpF porin.

摘要: Reassembly of OmpF porin from its denatured monomer into the sodium dodecyl sulfate-resistant species was investigated by using 27 kinds mild surfactants. Polyethyleneoxide-type surfactants with a hydrophilic-lipophilic balance value 10.8–14.6 induced trimerization porin. Dimerization and were non-polyethyleneoxide-type that are generally used for membrane protein solubilization. The dependence surfactant concentrations on reassembly estimated to obtain minimal concentration required protein. Extensive (∼85% yield) dimer (a putative assembly intermediate) observed at 0.05 mg/ml in 7 n-octyl-β-d-glucopyranoside 1 sulfate. This condition will be useful studies dimerization role mixed micelle system renaturation discussed.