Refolding and oriented insertion of a membrane protein into a lipid bilayer.

AUTOR(ES)

Surrey, T

RESUMO

We have studied the refolding and membrane insertion of the outer membrane protein OmpA of Escherichia coli. The protein was extracted from its native membrane by sonication in the presence of urea and dissolved in the urea/water mixture in unfolded form. In this form it was purified. Upon addition of preformed lipid vesicles, the protein spontaneously refolded and inserted into the vesicle membranes. The vesicles had to be small and the lipids had to be in the fluid state. The insertion occurred in an oriented manner.

Documentos Relacionados

• Membrane-promoted unfolding of acetylcholinesterase: A possible mechanism for insertion into the lipid bilayer
• Insertion of influenza M protein into the viral lipid bilayer and localization of site of insertion.
• Insertion of Influenza M Protein into the Viral Lipid Bilayer and Localization of Site of Insertion
• Photogating of ionic currents across a lipid bilayer.
• Use of an oriented transmembrane protein to probe the assembly of a supported phospholipid bilayer.