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

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Dynamic protein self-assembly driven by host–guest chemistry and the folding–unfolding feature of a mutually exclusive protein
Chemical Communications ( IF 4.3 ) Pub Date : 2017-09-04 00:00:00 , DOI: 10.1039/c7cc05745h
Ruidi Wang _{1,

2,

3,

4,

5} , Shanpeng Qiao _{1,

2,

3,

4,

5} , Linlu Zhao _{1,

2,

3,

4,

5} , Chunxi Hou _{1,

2,

3,

4,

5} , Xiumei Li _{1,

2,

3,

4,

5} , Yao Liu _{1,

2,

3,

4,

5} , Quan Luo _{1,

2,

3,

4,

5} , Jiayun Xu _{1,

2,

3,

4,

5} , Hongbin Li _{6,

7,

8,

9} , Junqiu Liu _{1,

2,

3,

4,

5}

Affiliation

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.

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