Observing folding pathways and kinetics of a single sodium-proton antiporter from Escherichia coli
Publikation: Beitrag in Fachzeitschrift › Forschungsartikel › Beigetragen › Begutachtung
Beitragende
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 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.
Details
Originalsprache | Englisch |
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Seiten (von - bis) | 2-8 |
Seitenumfang | 7 |
Fachzeitschrift | Journal of Molecular Biology |
Jahrgang | 355 |
Ausgabenummer | 1 |
Publikationsstatus | Veröffentlicht - 6 Jan. 2006 |
Peer-Review-Status | Ja |
Externe IDs
PubMed | 16298390 |
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Schlagworte
ASJC Scopus Sachgebiete
Schlagwörter
- Atomic force microscopy, Folding kinetics, Molecular interactions, Single-molecule force spectroscopy, Sodium/proton antiporter