Interactions of peptides with a protein pore.

Journal article

The partitioning of polypeptides into nanoscale transmembrane pores is of fundamental importance in biology. Examples include protein translocation in the endoplasmic reticulum and the passage of proteins through the nuclear pore complex. Here we examine the exchange of cationic alpha-helical peptides between the bulk aqueous phase and the transmembrane beta-barrel of the alpha-hemolysin (alphaHL) protein pore at the single-molecule level. The experimental kinetic data suggest a two-barrier, ...

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Authors: Movileanu, L; Schmittschmitt, J; Scholtz, J; Bayley, H

• Publication status: Published
• Journal: Biophysical journal
• Volume: 89
• Issue: 2
• Pages: 1030-1045
• Publication date: 2005-08-01
• DOI: 10.1529/biophysj.104.057406
• EISSN: 1542-0086
• ISSN: 0006-3495
• Language: English
• Keywords: Membrane Potentials; Bacterial Toxins; Models, Molecular; Lipid Bilayers; Protein Binding; Porosity; Ion Channel Gating; Membrane Fluidity; Models, Chemical; Hemolysin Proteins; Temperature; Binding Sites; Peptides; Computer Simulation