ArticlePloS one2013
Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Designing de novo TIM barrels: insights into stabilization, diversification, and functionalization strategies.Biochemical Society transactions · 2026Review
- Large-scale structure-informed multiple sequence alignment of proteins with SIMSApiper.Bioinformatics (Oxford, England) · 2024Article
- The Stability Landscape of de novo TIM Barrels Explored by a Modular Design Approach.Journal of molecular biology · 2021Article
- Evolution, folding, and design of TIM barrels and related proteins.Current opinion in structural biology · 2021Review
- Review
- Development and applications of artificial symmetrical proteins.Computational and structural biotechnology journal · 2020Review
- Selection and analyses of variants of a designed protein suggest importance of hydrophobicity of partially buried sidechains for protein stability at high temperatures.Protein science : a publication of the Protein Society · 2019Article
- In silico prediction of T- and B-cell epitopes in PmpD: First step towards to the design of a Chlamydia trachomatis vaccine.Biomedical journal · 2018Article
- Why reinvent the wheel? Building new proteins based on ready-made parts.Protein science : a publication of the Protein Society · 2016Review
- De novo design of a four-fold symmetric TIM-barrel protein with atomic-level accuracy.Nature chemical biology · 2016Article
- Design of symmetric TIM barrel proteins from first principles.BMC biochemistry · 2015Article
- Computational design of a self-assembling symmetrical β-propeller protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The computational protein design protocol Rosetta has been applied successfully to a wide variety of protein engineering problems. Here the aim was to test its ability to design de novo a protein adopting the TIM-barrel fold, whose formation requires about twice as many residues as in the largest proteins successfully designed de novo to date. The designed protein, Octarellin VI, contains 216 residues. Its amino acid composition is similar to that of natural TIM-barrel proteins. When produced and purified, it showed a far-UV circular dichroism spectrum characteristic of folded proteins, with α-helical and β-sheet secondary structure. Its stable tertiary structure was confirmed by both tryptophan fluorescence and circular dichroism in the near UV. It proved heat stable up to 70°C. Dynamic light scattering experiments revealed a unique population of particles averaging 4 nm in diameter, in good agreement with our model. Although these data suggest the successful creation of an artificial α/β protein of more than 200 amino acids, Octarellin VI shows an apparent noncooperative chemical unfolding and low solubility.
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Registered trials
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