Abstract
Atomic force microscopy (AFM) is a powerful imaging technique that allows recording topographical information of membrane proteins under near-physiological conditions. Remarkable results have been obtained on membrane proteins that were reconstituted into lipid bilayers. High-resolution AFM imaging of native disk membranes from vertebrate rod outer segments has unveiled the higher-order oligomeric state of the G protein-coupled receptor rhodopsin, which is highly expressed in disk membranes. Based on AFM imaging, it has been demonstrated that rhodopsin assembles in rows of dimers and paracrystals and that the rhodopsin dimer is the fundamental building block of higher-order structures.
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Acknowledgements
Financial support from the University of Bern, the Bern University Research Foundation, the Swiss National Science Foundation, and the National Centres of Competence in Research (NCCR) TransCure and Molecular Systems Engineering is gratefully acknowledged.
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Bosshart, P.D., Engel, A., Fotiadis, D. (2015). High-Resolution Atomic Force Microscopy Imaging of Rhodopsin in Rod Outer Segment Disk Membranes. In: Jastrzebska, B. (eds) Rhodopsin. Methods in Molecular Biology, vol 1271. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2330-4_13
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DOI: https://doi.org/10.1007/978-1-4939-2330-4_13
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