{"publisher":"Biophysical Society","oa":1,"abstract":[{"text":"Mechanical single-molecule techniques offer exciting possibilities to investigate protein folding and stability in native environments at submolecular resolution. By applying a free-energy reconstruction procedure developed by Hummer and Szabo, which is based on a statistical theorem introduced by Jarzynski, we determined the unfolding free energy of the membrane proteins bacteriorhodopsin (BR), halorhodopsin, and the sodium-proton antiporter NhaA. The calculated energies ranged from 290.5kcal/mol for BR to 485.5kcal/mol for NhaA. For the remarkably stable BR, the equilibrium unfolding free energy was independent of pulling rate and temperature ranging between 18 and 42°C. Our experiments also revealed heterogeneous energetic properties in individual transmembrane helices. In halorhodopsin, the stabilization of a short helical segment yielded a characteristic signature in the energy profile. In NhaA, a pronounced peak was observed at a functionally important site in the protein. Since a large variety of single- and multispan membrane proteins can be tackled in mechanical unfolding experiments, our approach provides a basis for systematically elucidating energetic properties of membrane proteins with the resolution of individual secondary-structure elements.","lang":"eng"}],"year":"2007","title":"Free energy of membrane protein unfolding derived from single-molecule force measurements","page":"930 - 937","type":"journal_article","day":"01","citation":{"ieee":"J. Preiner <i>et al.</i>, “Free energy of membrane protein unfolding derived from single-molecule force measurements,” <i>Biophysical Journal</i>, vol. 93, no. 3. Biophysical Society, pp. 930–937, 2007.","ama":"Preiner J, Janovjak HL, Rankl C, et al. Free energy of membrane protein unfolding derived from single-molecule force measurements. <i>Biophysical Journal</i>. 2007;93(3):930-937. doi:<a href=\"https://doi.org/10.1529/biophysj.106.096982\">10.1529/biophysj.106.096982</a>","apa":"Preiner, J., Janovjak, H. L., Rankl, C., Knaus, H., Cisneros, D., Kedrov, A., … Hinterdorfer, P. (2007). Free energy of membrane protein unfolding derived from single-molecule force measurements. <i>Biophysical Journal</i>. Biophysical Society. <a href=\"https://doi.org/10.1529/biophysj.106.096982\">https://doi.org/10.1529/biophysj.106.096982</a>","short":"J. Preiner, H.L. Janovjak, C. Rankl, H. Knaus, D. Cisneros, A. Kedrov, F. Kienberger, D. Mueller, P. Hinterdorfer, Biophysical Journal 93 (2007) 930–937.","ista":"Preiner J, Janovjak HL, Rankl C, Knaus H, Cisneros D, Kedrov A, Kienberger F, Mueller D, Hinterdorfer P. 2007. Free energy of membrane protein unfolding derived from single-molecule force measurements. Biophysical Journal. 93(3), 930–937.","mla":"Preiner, Johannes, et al. “Free Energy of Membrane Protein Unfolding Derived from Single-Molecule Force Measurements.” <i>Biophysical Journal</i>, vol. 93, no. 3, Biophysical Society, 2007, pp. 930–37, doi:<a href=\"https://doi.org/10.1529/biophysj.106.096982\">10.1529/biophysj.106.096982</a>.","chicago":"Preiner, Johannes, Harald L Janovjak, Christian Rankl, Helene Knaus, David Cisneros, Alexej Kedrov, Ferry Kienberger, Daniel Mueller, and Peter Hinterdorfer. “Free Energy of Membrane Protein Unfolding Derived from Single-Molecule Force Measurements.” <i>Biophysical Journal</i>. Biophysical Society, 2007. <a href=\"https://doi.org/10.1529/biophysj.106.096982\">https://doi.org/10.1529/biophysj.106.096982</a>."},"volume":93,"status":"public","date_updated":"2021-01-12T07:43:18Z","_id":"3411","publist_id":"2990","date_created":"2018-12-11T12:03:11Z","intvolume":"        93","extern":1,"issue":"3","quality_controlled":0,"date_published":"2007-08-01T00:00:00Z","publication":"Biophysical Journal","author":[{"last_name":"Preiner","first_name":"Johannes","full_name":"Preiner, Johannes"},{"orcid":"0000-0002-8023-9315","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","first_name":"Harald L","last_name":"Janovjak","full_name":"Harald Janovjak"},{"full_name":"Rankl, Christian","first_name":"Christian","last_name":"Rankl"},{"first_name":"Helene","last_name":"Knaus","full_name":"Knaus, Helene"},{"first_name":"David","last_name":"Cisneros","full_name":"Cisneros, David A"},{"first_name":"Alexej","last_name":"Kedrov","full_name":"Kedrov, Alexej"},{"last_name":"Kienberger","first_name":"Ferry","full_name":"Kienberger, Ferry"},{"full_name":"Mueller, Daniel J","last_name":"Mueller","first_name":"Daniel"},{"first_name":"Peter","last_name":"Hinterdorfer","full_name":"Hinterdorfer, Peter"}],"publication_status":"published","main_file_link":[{"open_access":"1","url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1913163/"}],"month":"08","doi":"10.1529/biophysj.106.096982"}