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

T Surrey, F Jähnig
Author Information
  1. T Surrey: Max-Planck-Institut für Biologie, Abteilung Membranbiochemie, Tübingen, Federal Republic of Germany.

Abstract

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.

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MeSH Term

Bacterial Outer Membrane Proteins
Cell Membrane
Circular Dichroism
Dimyristoylphosphatidylcholine
Electrophoresis, Polyacrylamide Gel
Endopeptidases
Escherichia coli
Lipid Bilayers
Models, Structural
Peptide Fragments
Protein Conformation
Recombinant Proteins
Spectrometry, Fluorescence
Tryptophan

Chemicals

Bacterial Outer Membrane Proteins
Lipid Bilayers
Peptide Fragments
Recombinant Proteins
Tryptophan
Endopeptidases
Dimyristoylphosphatidylcholine

Word Cloud

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