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Abstract | Cited by

A protein self-assembly nano-spring was developed through host–guest interactions between cucurbit[8]uril and tripeptide FGG tags of fusion protein FGG-recoverin-GST. Fine control of the conformational changes of the Ca2+-responsive domain allows for a 50% stretch of the protein nano-spring as it switches from the contracted state to the extended state.

Graphical abstract: An ion signal responsive dynamic protein nano-spring constructed by high ordered host–guest recognition

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