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Journal articles

High-Speed Force Spectroscopy for Single Protein Unfolding

Abstract : Single-molecule force spectroscopy (SMFS) measurements allow for quantification of the molecular forces required to unfold individual protein domains. Atomic force microscopy (AFM) is one of the long-established techniques for force spectroscopy (FS). Although FS at conventional AFM pulling rates provides valuable information on protein unfolding, in order to get a more complete picture of the mechanism, explore new regimes, and combine and compare experiments with simulations, we need higher pulling rates and μs-time resolution, now accessible via high-speed force spectroscopy (HS-FS). In this chapter, we provide a step-by-step protocol of HS-FS including sample preparation, measurements and analysis of the acquired data using HS-AFM with an illustrative example on unfolding of a well-studied concatamer made of eight repeats of the titin I91 domain.
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Contributor : Felix Rico Connect in order to contact the contributor
Submitted on : Friday, October 5, 2018 - 4:16:02 PM
Last modification on : Wednesday, November 3, 2021 - 4:44:43 AM
Long-term archiving on: : Sunday, January 6, 2019 - 5:00:21 PM


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Fidan Sumbul, Arin Marchesi, Hirohide Takahashi, Simon Scheuring, Felix Rico. High-Speed Force Spectroscopy for Single Protein Unfolding. Methods in Molecular Biology, Humana Press/Springer Imprint, 2018, pp.243-264. ⟨10.1007/978-1-4939-8591-3_15⟩. ⟨hal-01838371⟩



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