Jump to main content
Jump to site search

Issue 14, 2012
Previous Article Next Article

Single molecule force spectroscopy using polyproteins

Author affiliations


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

Back to tab navigation

Publication details

The article was received on 03 Feb 2012 and first published on 30 May 2012

Article type: Tutorial Review
DOI: 10.1039/C2CS35033E
Citation: Chem. Soc. Rev., 2012,41, 4781-4796
  •   Request permissions

    Single molecule force spectroscopy using polyproteins

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

Search articles by author