{"day":"01","publisher":"Biophysical Society","status":"public","year":"2005","page":"37 - 39","oa":1,"date_published":"2005-05-01T00:00:00Z","month":"05","date_created":"2018-12-11T12:03:13Z","citation":{"ieee":"H. L. Janovjak, T. Sapra, and D. Mueller, “Complex stability of single proteins explored by forced unfolding experiments,” <i>Biophysical Journal</i>, vol. 88, no. 5. Biophysical Society, pp. 37–39, 2005.","short":"H.L. Janovjak, T. Sapra, D. Mueller, Biophysical Journal 88 (2005) 37–39.","mla":"Janovjak, Harald L., et al. “Complex Stability of Single Proteins Explored by Forced Unfolding Experiments.” <i>Biophysical Journal</i>, vol. 88, no. 5, Biophysical Society, 2005, pp. 37–39, doi:<a href=\"https://doi.org/10.1529/biophysj.105.059774\">10.1529/biophysj.105.059774</a>.","ama":"Janovjak HL, Sapra T, Mueller D. Complex stability of single proteins explored by forced unfolding experiments. <i>Biophysical Journal</i>. 2005;88(5):37-39. doi:<a href=\"https://doi.org/10.1529/biophysj.105.059774\">10.1529/biophysj.105.059774</a>","apa":"Janovjak, H. L., Sapra, T., &#38; Mueller, D. (2005). Complex stability of single proteins explored by forced unfolding experiments. <i>Biophysical Journal</i>. Biophysical Society. <a href=\"https://doi.org/10.1529/biophysj.105.059774\">https://doi.org/10.1529/biophysj.105.059774</a>","ista":"Janovjak HL, Sapra T, Mueller D. 2005. Complex stability of single proteins explored by forced unfolding experiments. Biophysical Journal. 88(5), 37–39.","chicago":"Janovjak, Harald L, Tanuj Sapra, and Daniel Mueller. “Complex Stability of Single Proteins Explored by Forced Unfolding Experiments.” <i>Biophysical Journal</i>. Biophysical Society, 2005. <a href=\"https://doi.org/10.1529/biophysj.105.059774\">https://doi.org/10.1529/biophysj.105.059774</a>."},"quality_controlled":0,"title":"Complex stability of single proteins explored by forced unfolding experiments","main_file_link":[{"url":"http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1305525/","open_access":"1"}],"_id":"3416","doi":"10.1529/biophysj.105.059774","author":[{"first_name":"Harald L","full_name":"Harald Janovjak","orcid":"0000-0002-8023-9315","last_name":"Janovjak","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Sapra","full_name":"Sapra, Tanuj K","first_name":"Tanuj"},{"first_name":"Daniel","full_name":"Mueller, Daniel J","last_name":"Mueller"}],"abstract":[{"lang":"eng","text":"In the last decade atomic force microscopy has been used to measure the mechanical stability of single proteins. These force spectroscopy experiments have shown that many water-soluble and membrane proteins unfold via one or more intermediates. Recently, Li and co-workers found a linear correlation between the unfolding force of the native state and the intermediate in fibronectin, which they suggested indicated the presence of a molecular memory or multiple unfolding pathways (1). Here, we apply two independent methods in combination with Monte Carlo simulations to analyze the unfolding of α-helices E and D of bacteriorhodopsin (BR). We show that correlation analysis of unfolding forces is very sensitive to errors in force calibration of the instrument. In contrast, a comparison of relative forces provides a robust measure for the stability of unfolding intermediates. The proposed approach detects three energetically different states of α-helices E and D in trimeric BR. These states are not observed for monomeric BR and indicate that substantial information is hidden in forced unfolding experiments of single proteins."}],"publication_status":"published","publication":"Biophysical Journal","issue":"5","extern":1,"type":"journal_article","publist_id":"2985","date_updated":"2021-01-12T07:43:19Z","volume":88,"intvolume":"        88"}