Chapter title |
High-Speed Force Spectroscopy for Single Protein Unfolding
|
---|---|
Chapter number | 15 |
Book title |
Nanoscale Imaging
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-8591-3_15 |
Pubmed ID | |
Book ISBNs |
978-1-4939-8590-6, 978-1-4939-8591-3
|
Authors |
Fidan Sumbul, Arin Marchesi, Hirohide Takahashi, Simon Scheuring, Felix Rico, Sumbul, Fidan, Marchesi, Arin, Takahashi, Hirohide, Scheuring, Simon, Rico, Felix |
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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