ArticleACS synthetic biology2012
Proteins from an unevolved library of de novo designed sequences bind a range of small molecules.
Article in ACS synthetic biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- RNA and proteins joined up at the Origins of Life: Persistence is the point.bioRxiv : the preprint server for biology · 2026Article
- Article
- 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
- Review
- Hierarchical design of artificial proteins and complexes toward synthetic structural biology.Biophysical reviews · 2018Review
- Finding a Silver Bullet in a Stack of Proteins.Biochemistry · 2017Article
- Foldamer hypothesis for the growth and sequence differentiation of prebiotic polymers.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A de novo protein confers copper resistance in Escherichia coli.Protein science : a publication of the Protein Society · 2016Article
- A protein constructed de novo enables cell growth by altering gene regulation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- De Novo Proteins with Life-Sustaining Functions Are Structurally Dynamic.Journal of molecular biology · 2016Article
- Evolution of new functions de novo and from preexisting genes.Cold Spring Harbor perspectives in biology · 2015Review
- Divergent evolution of a bifunctional de novo protein.Protein science : a publication of the Protein Society · 2015Article
- Discovery of catalytic phages by biocatalytic self-assembly.Journal of the American Chemical Society · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The availability of large collections of de novo designed proteins presents new opportunities to harness novel macromolecules for synthetic biological functions. Many of these new functions will require binding to small molecules. Is the ability to bind small molecules a property that arises only in response to biological selection or computational design? Or alternatively, is small molecule binding a property of folded proteins that occurs readily amidst collections of unevolved sequences? These questions can be addressed by assessing the binding potential of de novo proteins that are designed to fold into stable structures, but are "naïve" in the sense that they (i) share no significant sequence similarity with natural proteins and (ii) were neither selected nor designed to bind small molecules. We chose three naïve proteins from a library of sequences designed to fold into 4-helix bundles and screened for binding to 10,000 compounds displayed on small molecule microarrays. Several binders were identified, and binding was characterized by a series of biophysical assays. Surprisingly, despite the similarity of the three de novo proteins to one another, they exhibit selective ligand binding. These findings demonstrate the potential of novel proteins for molecular recognition and have significant implications for a range of applications in synthetic biology.
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Registered trials
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