YidC from <i>Escherichia coli</i> Forms an Ion-Conducting Pore upon Activation by Ribosomes

YidC from <i>Escherichia coli</i> Forms an Ion-Conducting Pore upon Activation by Ribosomes

The universally conserved protein YidC aids in the insertion and folding of transmembrane polypeptides. Supposedly, a charged arginine faces its hydrophobic lipid core, facilitating polypeptide sliding along YidC’s surface. How the membrane barrier to other molecules may be maintained is unclear. He...

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Bibliographic Details
Main Authors: Denis G. Knyazev, Lukas Winter, Andreas Vogt, Sandra Posch, Yavuz Öztürk, Christine Siligan, Nikolaus Goessweiner-Mohr, Nora Hagleitner-Ertugrul, Hans-Georg Koch, Peter Pohl
Format: Article
Language:English
Published: MDPI AG 2023-12-01
Series:Biomolecules
Subjects:
protein translocation
fluorescence correlation spectroscopy
electrophysiology
single dye tracing
Online Access:https://www.mdpi.com/2218-273X/13/12/1774

Internet

https://www.mdpi.com/2218-273X/13/12/1774

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