Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein.
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 pr...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3747059?pdf=render |
| _version_ | 1828229729199587328 |
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| author | Maximiliano Figueroa Nicolas Oliveira Annabelle Lejeune Kristian W Kaufmann Brent M Dorr André Matagne Joseph A Martial Jens Meiler Cécile Van de Weerdt |
| author_facet | Maximiliano Figueroa Nicolas Oliveira Annabelle Lejeune Kristian W Kaufmann Brent M Dorr André Matagne Joseph A Martial Jens Meiler Cécile Van de Weerdt |
| author_sort | Maximiliano Figueroa |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T18:37:29Z |
| format | Article |
| id | doaj.art-1bd88007f61846ac98c74b30eb162b97 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-12T18:37:29Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-1bd88007f61846ac98c74b30eb162b972022-12-22T03:20:54ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0188e7185810.1371/journal.pone.0071858Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein.Maximiliano FigueroaNicolas OliveiraAnnabelle LejeuneKristian W KaufmannBrent M DorrAndré MatagneJoseph A MartialJens MeilerCécile Van de WeerdtThe 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.http://europepmc.org/articles/PMC3747059?pdf=render |
| spellingShingle | Maximiliano Figueroa Nicolas Oliveira Annabelle Lejeune Kristian W Kaufmann Brent M Dorr André Matagne Joseph A Martial Jens Meiler Cécile Van de Weerdt Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein. PLoS ONE |
| title | Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein. |
| title_full | Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein. |
| title_fullStr | Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein. |
| title_full_unstemmed | Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein. |
| title_short | Octarellin VI: using rosetta to design a putative artificial (β/α)8 protein. |
| title_sort | octarellin vi using rosetta to design a putative artificial β α 8 protein |
| url | http://europepmc.org/articles/PMC3747059?pdf=render |
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