Abstract
Total interference reflection fluorescence (TIRF) microscopy of lipid bilayers is an effective technique for studying the lateral movement and ion channel activity of single integral membrane proteins. Here we describe how to integrate the mitochondrial outer membrane preprotein translocase TOM-CC and its β-barrel protein-conducting channel Tom40 into supported lipid bilayers to identify possible relationships between movement and channel activity. We propose that our approach can be readily applied to membrane protein channels where transient tethering to either membrane-proximal or intramembrane structures is accompanied by a change in channel permeation.
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Acknowledgments
We thank Robin Ghosh for critically reviewing the manuscript. This work was supported in part by Laura Na Liu (2nd Physics Institute, University of Stuttgart) and by a grant from the Baden Württemberg Foundation (BiofMO-6 to SN).
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Wang, S., Nussberger, S. (2024). Tracking the Activity and Position of Mitochondrial β-Barrel Proteins. In: Ieva, R. (eds) Transmembrane β-Barrel Proteins. Methods in Molecular Biology, vol 2778. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3734-0_14
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DOI: https://doi.org/10.1007/978-1-0716-3734-0_14
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