Assembly of an in vitro synthesized Escherichia coli outer membrane porin into its stable trimeric configuration.

摘要: Abstract The folding of in vitro synthesized outer membrane protein PhoE Escherichia coli was studied immunoprecipitation experiments with monoclonal antibodies which recognize cell surface-exposed conformational epitopes. signal sequence appears to interfere the formation these epitopes, since a mutant lacks majority peptide could be precipitated four times better than wild type precursor. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis immunoprecipitated revealed that part present as heat-modifiable form migrated faster gels completely denatured protein. This probably represents folded monomer might an intermediate assembly Outer vesicles were required induce small amounts heat-stable trimers, functional vivo.