Issue 14, 2012
From the journal:

Chemical Society Reviews

Single molecule force spectroscopy using polyproteins

Toni Hoffmannab  and  Lorna Dougan*ab  

* Corresponding authors

a School of Physics and Astronomy, University of Leeds, Leeds LS2 9JT, United Kingdom

b Astbury Centre for Structural Molecular Biology and Institute of Molecular and Cellular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom
E-mail: l.dougan@leeds.ac.uk
Fax: +44 (0)113 343 3900
Tel: +44 (0)113 343 8958

Abstract

In recent years single molecule force spectroscopy has emerged as a powerful new tool to explore the mechanical stability and folding pathways of individual proteins. This technique is used to apply a stretching force between two points of a protein, unfolding the protein to an extended state. By measuring the unfolding and folding trajectories of individual proteins, insight can be gained into the physical mechanisms of protein folding. In this tutorial review we introduce the reader to single molecule force spectroscopy using the atomic force microscope (AFM), and explain the two main modes of operation of the AFM for force spectroscopy: force-extension and force-clamp. We introduce the approach of using polyproteins to obtain a clear mechanical fingerprint for monitoring the response of proteins to an applied mechanical force. In addition, we provide an informative and representative review of recent research on proteins using single molecule force spectroscopy. We focus on areas which have made a significant contribution to the single molecule protein folding field and highlight emerging areas of research which have wider implications for the general scientific community.

Graphical abstract: Single molecule force spectroscopy using polyproteins

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Article information

DOI
https://doi.org/10.1039/C2CS35033E
Article type
Tutorial Review
Submitted
03 Feb 2012
First published
30 May 2012

Chem. Soc. Rev., 2012,41, 4781-4796

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Single molecule force spectroscopy using polyproteins

T. Hoffmann and L. Dougan, Chem. Soc. Rev., 2012, 41, 4781 DOI: 10.1039/C2CS35033E

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