Issue 19, 2020

The nanomechanics of individual proteins


Mechanical forces regulate a large variety of cellular functionalities, encompassing e.g. motility, differentiation and muscle contractility. To adapt to the dynamic change in mechanical stress, the constitutive individual proteins need to reversibly stretch and recoil over long periods of time. Yet, the molecular mechanisms controlling the mechanical unfolding and refolding of proteins cannot be accessed by protein folding biochemistry experiments conducted in the bulk, because they cannot typically apply forces to individual proteins. The advent of single-molecule nanomechanical techniques, often combined with bespoke protein engineering strategies, has enabled monitoring the conformational dynamics of proteins under force with unprecedented length-, time- and force-resolution. This review focuses on the fundamental operational principles of the main single-molecule nanomechanical techniques, placing particular emphasis on the most common analytical approaches used to extract information directly from the experiments. The breadth of enabling applications highlights the most exciting and promising outputs from the nanomechanics field to date.

Graphical abstract: The nanomechanics of individual proteins

Article information

Article type
Tutorial Review
23 Apr 2020
First published
15 Sep 2020
This article is Open Access
Creative Commons BY license

Chem. Soc. Rev., 2020,49, 6816-6832

The nanomechanics of individual proteins

M. Mora, A. Stannard and S. Garcia-Manyes, Chem. Soc. Rev., 2020, 49, 6816 DOI: 10.1039/D0CS00426J

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