{"date_created":"2018-12-11T12:03:11Z","status":"public","author":[{"full_name":"Preiner, Johannes","last_name":"Preiner","first_name":"Johannes"},{"id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Harald Janovjak","last_name":"Janovjak","first_name":"Harald L","orcid":"0000-0002-8023-9315"},{"last_name":"Rankl","first_name":"Christian","full_name":"Rankl, Christian"},{"full_name":"Knaus, Helene","last_name":"Knaus","first_name":"Helene"},{"last_name":"Cisneros","first_name":"David","full_name":"Cisneros, David A"},{"full_name":"Kedrov, Alexej","first_name":"Alexej","last_name":"Kedrov"},{"first_name":"Ferry","last_name":"Kienberger","full_name":"Kienberger, Ferry"},{"full_name":"Mueller, Daniel J","first_name":"Daniel","last_name":"Mueller"},{"full_name":"Hinterdorfer, Peter","first_name":"Peter","last_name":"Hinterdorfer"}],"date_updated":"2021-01-12T07:43:18Z","publist_id":"2990","volume":93,"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"}],"_id":"3411","oa":1,"type":"journal_article","page":"930 - 937","doi":"10.1529/biophysj.106.096982","issue":"3","publication_status":"published","publication":"Biophysical Journal","title":"Free energy of membrane protein unfolding derived from single-molecule force measurements","quality_controlled":0,"main_file_link":[{"open_access":"1","url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1913163/"}],"intvolume":"        93","citation":{"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>","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.","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>.","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.","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>","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.","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>."},"extern":1,"date_published":"2007-08-01T00:00:00Z","month":"08","year":"2007","day":"01","publisher":"Biophysical Society"}