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The life of proteins under mechanical force

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Although much of our understanding of protein folding comes from studies of isolated protein domains in bulk, in the cellular environment the intervention of external molecular machines is essential during the protein life cycle. During the past decade single molecule force spectroscopy techniques have been extremely useful to deepen our understanding of these interventional molecular processes, as they allow for monitoring and manipulating mechanochemical events in individual protein molecules. Here, we review some of the critical steps in the protein life cycle, starting with the biosynthesis of the nascent polypeptide chain in the ribosome, continuing with the folding supported by chaperones and the translocation into different cell compartments, and ending with proteolysis in the proteasome. Along these steps, proteins experience molecular forces often combined with chemical transformations, affecting their folding and structure, which are measured or mimicked in the laboratory by the application of force with a single molecule apparatus. These mechanochemical reactions can potentially be used as targets for fighting against diseases. Inspired by these insightful experiments, we devise an outlook on the emerging field of mechanopharmacology, which reflects an alternative paradigm for drug design.

Graphical abstract: The life of proteins under mechanical force

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Publication details

The article was received on 30 Nov 2017 and first published on 23 Feb 2018

Article type: Review Article
DOI: 10.1039/C7CS00820A
Citation: Chem. Soc. Rev., 2018, Advance Article
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    The life of proteins under mechanical force

    J. Schönfelder, A. Alonso-Caballero, D. De Sancho and R. Perez-Jimenez, Chem. Soc. Rev., 2018, Advance Article , DOI: 10.1039/C7CS00820A

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