PMID:16298390

Citation	Kedrov, A, Janovjak, H, Ziegler, C, Kuhlbrandt, W and Muller, DJ (2006) Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli. J. Mol. Biol. 355:2-8
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 a single NhaA polypeptide forming structural segments such as the Na+-binding site, transmembrane alpha-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.
Links	PubMed Online version:10.1016/j.jmb.2005.10.028
Keywords	Binding Sites; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Kinetics; Microscopy, Atomic Force; Protein Folding; Protein Structure, Secondary; Sodium-Hydrogen Antiporter/chemistry; Sodium-Hydrogen Antiporter/metabolism
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Add links to pages that link here (e.g. gene, product, method pages)

See Help:References for how to manage references in EcoliWiki.