{"article_processing_charge":"No","citation":{"ieee":"C. P. Goodrich et al., “Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations,” The Journal of Physical Chemistry B, vol. 111, no. 13. American Chemical Society, pp. 3332–3335, 2007.","short":"C.P. Goodrich, S. Kirmizialtin, B.M. Huyghues-Despointes, A. Zhu, J.M. Scholtz, D.E. Makarov, L. Movileanu, The Journal of Physical Chemistry B 111 (2007) 3332–3335.","mla":"Goodrich, Carl Peter, et al. “Single-Molecule Electrophoresis of β-Hairpin Peptides by Electrical Recordings and Langevin Dynamics Simulations.” The Journal of Physical Chemistry B, vol. 111, no. 13, American Chemical Society, 2007, pp. 3332–35, doi:10.1021/jp071364h.","ama":"Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, et al. Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. The Journal of Physical Chemistry B. 2007;111(13):3332-3335. doi:10.1021/jp071364h","apa":"Goodrich, C. P., Kirmizialtin, S., Huyghues-Despointes, B. M., Zhu, A., Scholtz, J. M., Makarov, D. E., & Movileanu, L. (2007). Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. The Journal of Physical Chemistry B. American Chemical Society. https://doi.org/10.1021/jp071364h","chicago":"Goodrich, Carl Peter, Serdal Kirmizialtin, Beatrice M. Huyghues-Despointes, Aiping Zhu, J. Martin Scholtz, Dmitrii E. Makarov, and Liviu Movileanu. “Single-Molecule Electrophoresis of β-Hairpin Peptides by Electrical Recordings and Langevin Dynamics Simulations.” The Journal of Physical Chemistry B. American Chemical Society, 2007. https://doi.org/10.1021/jp071364h.","ista":"Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, Zhu A, Scholtz JM, Makarov DE, Movileanu L. 2007. Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. The Journal of Physical Chemistry B. 111(13), 3332–3335."},"month":"03","date_created":"2020-04-30T12:19:15Z","status":"public","publisher":"American Chemical Society","article_type":"original","year":"2007","page":"3332-3335","day":"13","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_published":"2007-03-13T00:00:00Z","date_updated":"2021-01-12T08:15:29Z","volume":111,"extern":"1","type":"journal_article","publication_identifier":{"issn":["1520-6106","1520-5207"]},"intvolume":" 111","language":[{"iso":"eng"}],"_id":"7780","author":[{"id":"EB352CD2-F68A-11E9-89C5-A432E6697425","last_name":"Goodrich","orcid":"0000-0002-1307-5074","full_name":"Goodrich, Carl Peter","first_name":"Carl Peter"},{"last_name":"Kirmizialtin","first_name":"Serdal","full_name":"Kirmizialtin, Serdal"},{"full_name":"Huyghues-Despointes, Beatrice M.","first_name":"Beatrice M.","last_name":"Huyghues-Despointes"},{"full_name":"Zhu, Aiping","first_name":"Aiping","last_name":"Zhu"},{"full_name":"Scholtz, J. Martin","first_name":"J. Martin","last_name":"Scholtz"},{"full_name":"Makarov, Dmitrii E.","first_name":"Dmitrii E.","last_name":"Makarov"},{"last_name":"Movileanu","first_name":"Liviu","full_name":"Movileanu, Liviu"}],"doi":"10.1021/jp071364h","quality_controlled":"1","title":"Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations","issue":"13","publication":"The Journal of Physical Chemistry B","publication_status":"published","abstract":[{"lang":"eng","text":"We used single-channel electrical recordings and Langevin molecular dynamics simulations to explore the electrophoretic translocation of various β-hairpin peptides across the staphylococcal α-hemolysin (αHL) protein pore at single-molecule resolution. The β-hairpin peptides, which varied in their folding properties, corresponded to the C terminal residues of the B1 domain of protein G. The translocation time was strongly dependent on the electric force and was correlated with the folding features of the β-hairpin peptides. Highly unfolded peptides entered the pore in an extended conformation, resulting in fast single-file translocation events. In contrast, the translocation of the folded β-hairpin peptides occurred more slowly. In this case, the β-hairpin peptides traversed the αHL pore in a misfolded or fully folded conformation. This study demonstrates that the interaction between a polypeptide and a β-barrel protein pore is dependent on the folding features of the polypeptide. "}],"oa_version":"None"}