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Protein machines

An open and shut cage

Nature Nanotechnology volume 8, pages 892–893 (2013)Cite this article

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By incorporating photosensitive switches, protein nanocages can be made to open and close on demand with light.

Proteins can self-assemble into nanoscale machines that exhibit sophisticated functional properties such as molecular recognition, and can perform work using chemical energy, typically obtained from the hydrolysis of adenosine triphosphate (ATP). Chaperonins are a class of protein machines whose natural function is to facilitate the folding of other proteins and are composed of two rings of protein subunits that self-assemble into a cage-like structure. This cage can be opened and closed by the binding and hydrolysis of ATP.

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Figure 1: Turning an ATP-driven chaperonin into a light-driven nanocage.

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Authors and Affiliations

  1. G. Andrew Woolley is at the Department of Chemistry, University of Toronto, Ontario M5S 3H6, Canada,

    G. Andrew Woolley

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  1. G. Andrew Woolley
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Correspondence to G. Andrew Woolley.

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Woolley, G. An open and shut cage. Nature Nanotech 8, 892–893 (2013). https://doi.org/10.1038/nnano.2013.260

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  • DOI: https://doi.org/10.1038/nnano.2013.260

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