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

TitleDynamic protein self-assembly driven by host-guest chemistry and the folding-unfolding feature of a mutually exclusive protein
Publication TypeJournal Article
Year of Publication2017
AuthorsWang, R, Qiao, S, Zhao, L, Hou, C, Li, X, Liu, Y, Luo, Q, Xu, J, Li, H, Liu, J
JournalCHEMICAL COMMUNICATIONS
Volume53
Pagination10532-10535
Date PublishedSEP 28
ISSN1359-7345
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.

DOI10.1039/c7cc05745h