ArticleProtein science : a publication of the Protein Society2012
Designing redox potential-controlled protein switches based on mutually exclusive proteins.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Seesaw protein: Design of a protein that adopts interconvertible alternative functional conformations and its dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Engineering protein polymers of ultrahigh molecular weightChemical science · 2019Article
- Influence of Secondary-Structure Folding on the Mutually Exclusive Folding Process of GL5/I27 Protein: Evidence from Molecular Dynamics Simulations.International journal of molecular sciences · 2016Article
- Rational design of a fusion protein to exhibit disulfide-mediated logic gate behavior.ACS synthetic biology · 2015Article
- Tuning response curves for synthetic biology.ACS synthetic biology · 2013Article
- Regulated unfolding of proteins in signaling.FEBS letters · 2013Review
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Authors and funding
4 authors.
Funding
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Abstract
Synthetic/artificial protein switches provide an efficient means of controlling protein functions using chemical signals and stimuli. Mutually exclusive proteins, in which only the host or guest domain can remain folded at a given time owing to conformational strain, have been used to engineer novel protein switches that can switch enzymatic functions on and off in response to ligand binding. To further explore the potential of mutually exclusive proteins as protein switches and sensors, we report here a new redox-based approach to engineer a mutually exclusive folding-based protein switch. By introducing a disulfide bond into the host domain of a mutually exclusive protein, we demonstrate that it is feasible to use redox potential to switch the host domain between its folded and unfolded conformations via the mutually exclusive folding mechanism, and thus switching the functionality of the host domain on and off. Our study opens a new and potentially general avenue that uses mutually exclusive proteins to design novel switches able to control the function of a variety of proteins.
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