ArticleProtein science : a publication of the Protein Society2011
Binding of small molecules to cavity forming mutants of a de novo designed protein.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A de novo protein catalyzes the synthesis of semiconductor quantum dots.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A de novo protein confers copper resistance in Escherichia coli.Protein science : a publication of the Protein Society · 2016Article
- Divergent evolution of a bifunctional de novo protein.Protein science : a publication of the Protein Society · 2015Article
- Designing allosteric control into enzymes by chemical rescue of structure.Journal of the American Chemical Society · 2012Article
- Proteins from an unevolved library of de novo designed sequences bind a range of small molecules.ACS synthetic biology · 2012Article
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Authors and funding
4 authors.
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Abstract
A central goal of protein design is to devise novel proteins for applications in biotechnology and medicine. Many applications, including those focused on sensing and catalysis will require proteins that recognize and bind to small molecules. Here, we show that stably folded α-helical proteins isolated from a binary patterned library of designed sequences can be mutated to produce binding sites capable of binding a range of small aromatic compounds. Specifically, we mutated two phenylalanine side chains to alanine in the known structure of de novo protein S-824 to create buried cavities in the core of this four-helix bundle. The parental protein and the Phe→Ala variants were exposed to mixtures of compounds, and selective binding was assessed by saturation transfer difference NMR. The affinities of benzene and a number of its derivatives were determined by pulse field gradient spin echo NMR, and several of the compounds were shown to bind the mutated protein with micromolar dissociation constants. These studies suggest that stably folded de novo proteins from binary patterned libraries are well-suited as scaffolds for the design of binding sites.
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