title: Peptide translocation through the mesoscopic channel: binding kinetics at the single molecule level.
abstract: Single channel electrophysiological studies have been carried out to elucidate the underlying interactions during the translocation of polypeptides through protein channels. For this we used OmpF from the outer cell membrane of E. coli and arginine-based peptides of different charges, lengths and covalently linked polyethylene glycol as a model system. In order to reveal the fast kinetics of peptide binding, we performed a temperature scan. Together with the voltage-dependent single-channel conductance, we quantify peptide binding and translocation.
authors.affiliation: School of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759, Bremen, Germany.
authors.forename: Usha
authors.initials: U
authors.lastname: Lamichhane
authors.forename: Tuhidul
authors.initials: T
authors.lastname: Islam
authors.forename: Sonal
authors.initials: S
authors.lastname: Prasad
authors.forename: Helge
authors.initials: H
authors.lastname: Weingart
authors.forename: Kozhinjampara R
authors.initials: KR
authors.lastname: Mahendran
authors.forename: Mathias
authors.initials: M
authors.lastname: Winterhalter
mesh_terms: D002462:Cell Membrane / Q000378:metabolism; D055724:Electrophysiological Phenomena; D004926:Escherichia coli / Q000166:cytology; D007700:Kinetics; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000737:chemistry; D018272:Porins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D021381:Protein Transport; D013696:Temperature; D013816:Thermodynamics
chemical_list: C109237:OmpF protein; D010455:Peptides; D018272:Porins; D011092:Polyethylene Glycols