Abstract
Membrane proteins are an important class of proteins in biology and therapeutics. Understanding the dynamic nature of the molecular interactions that stabilize membrane protein structure is critical to dissect the mechanism of action and dysfunction of these proteins. Single-molecule force spectroscopy (SMFS) and dynamic SMFS (DFS) are emerging nanotechniques that allow the study of membrane proteins under the physiologically relevant conditions of a lipid bilayer and buffer conditions. These techniques directly probe the molecular interactions underlying protein structure and reveal unique insights about their properties. Outlined in this report will be procedures on how to conduct SMFS and DFS on rhodopsin in native retinal membranes. Rhodopsin is a membrane protein belonging to the G protein-coupled receptor family of proteins, one of the largest families of proteins in nature.
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Acknowledgments
This work was funded by the European Community’s Seventh Framework Programme [FP7/2007–2013] under grant agreement n° [211800], Swiss National Science Foundation, National Institutes of Health (R01EY021731), and Research to Prevent Blindness (Career Development Award).
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Park, P.SH., Müller, D.J. (2015). Dynamic Single-Molecule Force Spectroscopy of Rhodopsin in Native 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_12
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DOI: https://doi.org/10.1007/978-1-4939-2330-4_12
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