Evidence for a Loop-Like Insertion Mechanism of Pro-Omp A into the Inner Membrane of Escherichia Coli
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1994.00891.x/fullpdf
Reference37 articles.
1. A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coli.
2. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.
3. Penetration of the signal sequence of Escherichia coli PhoE protein into phospholipid model membranes leads to lipid-specific changes in signal peptide structure and alterations of lipid organization
4. Conformations of Signal Peptides Induced by Lipids Suggest Initial Steps in Protein Export
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