Abstract
Atomic force microscopy (AFM)-based single-molecule force spectroscopy allows direct physical manipulation of single membrane proteins under near-physiological conditions. It can be applied to study mechanical properties and molecular interactions as well as unfolding and folding pathways of membrane proteins. Here, we describe the basic procedure to study membrane proteins by single-molecule force spectroscopy and discuss general requirements of the experimental setup as well as common pitfalls typically encountered when working with membrane proteins in AFM.
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Acknowledgment
We thank Nico Strohmeyer for proofreading the manuscript. Johannes Thoma was supported by a long-term European Molecular Biology Organization (EMBO) fellowship (ALTF 413-2018).
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Ritzmann, N., Thoma, J. (2020). Mechanical Unfolding and Refolding of Single Membrane Proteins by Atomic Force Microscopy. In: Perez, C., Maier, T. (eds) Expression, Purification, and Structural Biology of Membrane Proteins. Methods in Molecular Biology, vol 2127. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0373-4_23
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DOI: https://doi.org/10.1007/978-1-0716-0373-4_23
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