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Issue 76, 2017
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Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein

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Abstract

A novel exploration utilizing a well-designed fusion protein containing a redox stimuli-responsive domain was developed to construct dynamic protein self-assemblies induced by cucurbit[8]uril-based supramolecular interactions. The reversible interconversion of the morphology of the assemblies between nanowires and nanorings was regulated precisely by redox conditions.

Graphical abstract: Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein

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Publication details

The article was received on 24 Jul 2017, accepted on 04 Sep 2017 and first published on 04 Sep 2017


Article type: Communication
DOI: 10.1039/C7CC05745H
Citation: Chem. Commun., 2017,53, 10532-10535
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    Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein

    R. Wang, S. Qiao, L. Zhao, C. Hou, X. Li, Y. Liu, Q. Luo, J. Xu, H. Li and J. Liu, Chem. Commun., 2017, 53, 10532
    DOI: 10.1039/C7CC05745H

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