{"type":"journal_article","day":"06","citation":{"mla":"Kedrov, Alexej, et al. “Observing Folding Pathways and Kinetics of a Single Sodium-Proton Antiporter from Escherichia Coli.” <i>Journal of Molecular Biology</i>, vol. 355, no. 1, Elsevier, 2006, pp. 2–8, doi:<a href=\"https://doi.org/10.1016/j.jmb.2005.10.028\">10.1016/j.jmb.2005.10.028</a>.","ama":"Kedrov A, Janovjak HL, Ziegler C, Kühlbrandt W, Mueller D. Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. <i>Journal of Molecular Biology</i>. 2006;355(1):2-8. doi:<a href=\"https://doi.org/10.1016/j.jmb.2005.10.028\">10.1016/j.jmb.2005.10.028</a>","short":"A. Kedrov, H.L. Janovjak, C. Ziegler, W. Kühlbrandt, D. Mueller, Journal of Molecular Biology 355 (2006) 2–8.","chicago":"Kedrov, Alexej, Harald L Janovjak, Christine Ziegler, Werner Kühlbrandt, and Daniel Mueller. “Observing Folding Pathways and Kinetics of a Single Sodium-Proton Antiporter from Escherichia Coli.” <i>Journal of Molecular Biology</i>. Elsevier, 2006. <a href=\"https://doi.org/10.1016/j.jmb.2005.10.028\">https://doi.org/10.1016/j.jmb.2005.10.028</a>.","ista":"Kedrov A, Janovjak HL, Ziegler C, Kühlbrandt W, Mueller D. 2006. Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. Journal of Molecular Biology. 355(1), 2–8.","apa":"Kedrov, A., Janovjak, H. L., Ziegler, C., Kühlbrandt, W., &#38; Mueller, D. (2006). Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2005.10.028\">https://doi.org/10.1016/j.jmb.2005.10.028</a>","ieee":"A. Kedrov, H. L. Janovjak, C. Ziegler, W. Kühlbrandt, and D. Mueller, “Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli,” <i>Journal of Molecular Biology</i>, vol. 355, no. 1. Elsevier, pp. 2–8, 2006."},"status":"public","year":"2006","extern":1,"volume":355,"_id":"3414","publication":"Journal of Molecular Biology","date_updated":"2021-01-12T07:43:19Z","date_created":"2018-12-11T12:03:12Z","page":"2 - 8","abstract":[{"lang":"eng","text":"Mechanisms of folding and misfolding of membrane proteins are of interest in cell biology. Recently, we have established single-molecule force spectroscopy to observe directly the stepwise folding of the Na+/H+antiporter NhaA from Escherichia coli in vitro. Here, we improved this approach significantly to track the folding intermediates of asingle NhaA polypeptide forming structural segments such as the Na+-binding site, transmembrane α-helices, and helical pairs. The folding rates of structural segments ranged from 0.31 s−1 to 47 s−1, providing detailed insight into a distinct folding hierarchy of an unfolded polypeptide into the native membrane protein structure. In some cases, however, the folding chain formed stable and kinetically trapped non-native structures, which could be assigned to misfolding events of the antiporter."}],"date_published":"2006-01-06T00:00:00Z","title":"Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli","doi":"10.1016/j.jmb.2005.10.028","publication_status":"published","author":[{"last_name":"Kedrov","first_name":"Alexej","full_name":"Kedrov, Alexej"},{"last_name":"Janovjak","first_name":"Harald L","full_name":"Harald Janovjak","orcid":"0000-0002-8023-9315","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Ziegler,  Christine","first_name":"Christine","last_name":"Ziegler"},{"last_name":"Kühlbrandt","full_name":"Kühlbrandt, Werner","first_name":"Werner"},{"full_name":"Mueller, Daniel J","first_name":"Daniel","last_name":"Mueller"}],"month":"01","intvolume":"       355","quality_controlled":0,"issue":"1","publisher":"Elsevier","publist_id":"2987"}