{"publication_identifier":{"issn":["1520-6106","1520-5207"]},"author":[{"first_name":"Carl Peter","last_name":"Goodrich","full_name":"Goodrich, Carl Peter","orcid":"0000-0002-1307-5074","id":"EB352CD2-F68A-11E9-89C5-A432E6697425"},{"first_name":"Serdal","last_name":"Kirmizialtin","full_name":"Kirmizialtin, Serdal"},{"full_name":"Huyghues-Despointes, Beatrice M.","last_name":"Huyghues-Despointes","first_name":"Beatrice M."},{"full_name":"Zhu, Aiping","last_name":"Zhu","first_name":"Aiping"},{"last_name":"Scholtz","full_name":"Scholtz, J. Martin","first_name":"J. Martin"},{"first_name":"Dmitrii E.","last_name":"Makarov","full_name":"Makarov, Dmitrii E."},{"first_name":"Liviu","full_name":"Movileanu, Liviu","last_name":"Movileanu"}],"language":[{"iso":"eng"}],"article_processing_charge":"No","status":"public","date_created":"2020-04-30T12:19:15Z","extern":"1","_id":"7780","type":"journal_article","citation":{"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.” <i>The Journal of Physical Chemistry B</i>. American Chemical Society, 2007. <a href=\"https://doi.org/10.1021/jp071364h\">https://doi.org/10.1021/jp071364h</a>.","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.","apa":"Goodrich, C. P., Kirmizialtin, S., Huyghues-Despointes, B. M., Zhu, A., Scholtz, J. M., Makarov, D. E., &#38; Movileanu, L. (2007). Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. <i>The Journal of Physical Chemistry B</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/jp071364h\">https://doi.org/10.1021/jp071364h</a>","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.","ieee":"C. P. Goodrich <i>et al.</i>, “Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations,” <i>The Journal of Physical Chemistry B</i>, vol. 111, no. 13. American Chemical Society, pp. 3332–3335, 2007.","ama":"Goodrich CP, Kirmizialtin S, Huyghues-Despointes BM, et al. Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations. <i>The Journal of Physical Chemistry B</i>. 2007;111(13):3332-3335. doi:<a href=\"https://doi.org/10.1021/jp071364h\">10.1021/jp071364h</a>","mla":"Goodrich, Carl Peter, et al. “Single-Molecule Electrophoresis of β-Hairpin Peptides by Electrical Recordings and Langevin Dynamics Simulations.” <i>The Journal of Physical Chemistry B</i>, vol. 111, no. 13, American Chemical Society, 2007, pp. 3332–35, doi:<a href=\"https://doi.org/10.1021/jp071364h\">10.1021/jp071364h</a>."},"year":"2007","volume":111,"oa_version":"None","day":"13","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publisher":"American Chemical Society","quality_controlled":"1","date_updated":"2021-01-12T08:15:29Z","publication":"The Journal of Physical Chemistry B","doi":"10.1021/jp071364h","intvolume":"       111","page":"3332-3335","date_published":"2007-03-13T00:00:00Z","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. "}],"article_type":"original","issue":"13","title":"Single-molecule electrophoresis of β-hairpin peptides by electrical recordings and Langevin dynamics simulations","month":"03","publication_status":"published"}