Abstract
Atomic force microscopy in its single-molecule force spectroscopy mode is a nanomanipulation technique that is extensively used for the study of the mechanical properties of proteins. It is particularly suited to examine their response to stretching (i.e., molecular elasticity and mechanical stability). Here, we describe protein engineering strategies and single-molecule AFM techniques for probing protein mechanics, with special emphasis on polycystic kidney disease (PKD) proteins. We also provide step-by-step protocols for preparing proteins and performing single-molecule force measurements.
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Acknowledgments
This work was funded by NIH grant R01DK073394, the John Sealy Memorial Endowment Fund for Biomedical Research, and by the Polycystic Kidney Foundation (grant 116a2r).
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Ma, L., Xu, M., Oberhauser, A.F. (2012). Single-Molecule Force Spectroscopy of Polycystic Kidney Disease Proteins. In: Bujalowski, W. (eds) Spectroscopic Methods of Analysis. Methods in Molecular Biology, vol 875. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-61779-806-1_16
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DOI: https://doi.org/10.1007/978-1-61779-806-1_16
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