--- res: bibo_abstract: - 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.@eng bibo_authorlist: - foaf_Person: foaf_givenName: Alexej foaf_name: Kedrov, Alexej foaf_surname: Kedrov - foaf_Person: foaf_givenName: Harald L foaf_name: Harald Janovjak foaf_surname: Janovjak foaf_workInfoHomepage: http://www.librecat.org/personId=33BA6C30-F248-11E8-B48F-1D18A9856A87 orcid: 0000-0002-8023-9315 - foaf_Person: foaf_givenName: Christine foaf_name: Ziegler, Christine foaf_surname: Ziegler - foaf_Person: foaf_givenName: Werner foaf_name: Kühlbrandt, Werner foaf_surname: Kühlbrandt - foaf_Person: foaf_givenName: Daniel foaf_name: Mueller, Daniel J foaf_surname: Mueller bibo_doi: 10.1016/j.jmb.2005.10.028 bibo_issue: '1' bibo_volume: 355 dct_date: 2006^xs_gYear dct_publisher: Elsevier@ dct_title: Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli@ ...