{"extern":1,"type":"journal_article","date_updated":"2021-01-12T07:43:20Z","publist_id":"2982","volume":12,"intvolume":"        12","quality_controlled":0,"title":"Probing the energy landscape of the membrane protein bacteriorhodopsin","_id":"3419","doi":"10.1016/j.str.2004.03.016","author":[{"last_name":"Janovjak","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Harald Janovjak","first_name":"Harald L","orcid":"0000-0002-8023-9315"},{"last_name":"Struckmeier","first_name":"Jens","full_name":"Struckmeier, Jens"},{"full_name":"Hubain, Maurice","first_name":"Maurice","last_name":"Hubain"},{"last_name":"Kessler","full_name":"Kessler, Max","first_name":"Max"},{"last_name":"Kedrov","first_name":"Alexej","full_name":"Kedrov, Alexej"},{"first_name":"Daniel","full_name":"Mueller, Daniel J","last_name":"Mueller"}],"abstract":[{"lang":"eng","text":"The folding and stability of transmembrane proteins is a fundamental and unsolved biological problem. Here, single bacteriorhodopsin molecules were mechanically unfolded from native purple membranes using atomic force microscopy and force spectroscopy. The energy landscape of individual transmembrane α helices and polypeptide loops was mapped by monitoring the pulling speed dependence of the unfolding forces and applying Monte Carlo simulations. Single helices formed independently stable units stabilized by a single potential barrier. Mechanical unfolding of the helices was triggered by 3.9–7.7 Å extension, while natural unfolding rates were of the order of 10−3 s−1. Besides acting as individually stable units, helices associated pairwise, establishing a collective potential barrier. The unfolding pathways of individual proteins reflect distinct pulling speed-dependent unfolding routes in their energy landscapes. These observations support the two-stage model of membrane protein folding in which α helices insert into the membrane as stable units and then assemble into the functional protein."}],"publication":"Structure","issue":"5","publication_status":"published","month":"05","date_created":"2018-12-11T12:03:14Z","citation":{"ista":"Janovjak HL, Struckmeier J, Hubain M, Kessler M, Kedrov A, Mueller D. 2004. Probing the energy landscape of the membrane protein bacteriorhodopsin. Structure. 12(5), 871–879.","chicago":"Janovjak, Harald L, Jens Struckmeier, Maurice Hubain, Max Kessler, Alexej Kedrov, and Daniel Mueller. “Probing the Energy Landscape of the Membrane Protein Bacteriorhodopsin.” <i>Structure</i>. Cell Press, 2004. <a href=\"https://doi.org/10.1016/j.str.2004.03.016\">https://doi.org/10.1016/j.str.2004.03.016</a>.","apa":"Janovjak, H. L., Struckmeier, J., Hubain, M., Kessler, M., Kedrov, A., &#38; Mueller, D. (2004). Probing the energy landscape of the membrane protein bacteriorhodopsin. <i>Structure</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.str.2004.03.016\">https://doi.org/10.1016/j.str.2004.03.016</a>","ama":"Janovjak HL, Struckmeier J, Hubain M, Kessler M, Kedrov A, Mueller D. Probing the energy landscape of the membrane protein bacteriorhodopsin. <i>Structure</i>. 2004;12(5):871-879. doi:<a href=\"https://doi.org/10.1016/j.str.2004.03.016\">10.1016/j.str.2004.03.016</a>","mla":"Janovjak, Harald L., et al. “Probing the Energy Landscape of the Membrane Protein Bacteriorhodopsin.” <i>Structure</i>, vol. 12, no. 5, Cell Press, 2004, pp. 871–79, doi:<a href=\"https://doi.org/10.1016/j.str.2004.03.016\">10.1016/j.str.2004.03.016</a>.","short":"H.L. Janovjak, J. Struckmeier, M. Hubain, M. Kessler, A. Kedrov, D. Mueller, Structure 12 (2004) 871–879.","ieee":"H. L. Janovjak, J. Struckmeier, M. Hubain, M. Kessler, A. Kedrov, and D. Mueller, “Probing the energy landscape of the membrane protein bacteriorhodopsin,” <i>Structure</i>, vol. 12, no. 5. Cell Press, pp. 871–879, 2004."},"day":"01","status":"public","publisher":"Cell Press","year":"2004","page":"871 - 879","date_published":"2004-05-01T00:00:00Z"}