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Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Kedrov A,Janovjak H,Ziegler C,Kuhlbrandt W,Muller DJ

doi

10.1016/j.jmb.2005.10.028

keywords:

subject

Has Abstract

pub_date

2006-01-06 00:00:00

pages

2-8

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)01259-3

journal_volume

355

pub_type

杂志文章

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