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.
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Acknowledgments
The authors acknowledge the DFG for financial support through Wi2278/18-1. Special thanks to Niraj Modi for providing the structural schema of OmpF.
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Lamichhane, U., Islam, T., Prasad, S. et al. Peptide translocation through the mesoscopic channel: binding kinetics at the single molecule level. Eur Biophys J 42, 363–369 (2013). https://doi.org/10.1007/s00249-012-0885-6
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DOI: https://doi.org/10.1007/s00249-012-0885-6