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Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Proceedings of the National Academy of Sciences, 110, 2013, 6, S. 2135-2139 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Longo, Liam M. Lee, Jihun Blaber, Michael Longo, Liam M. Lee, Jihun Blaber, Michael |
|---|---|
| author |
Longo, Liam M. Lee, Jihun Blaber, Michael |
| spellingShingle |
Longo, Liam M. Lee, Jihun Blaber, Michael Proceedings of the National Academy of Sciences Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein Multidisciplinary |
| author_sort |
longo, liam m. |
| spelling |
Longo, Liam M. Lee, Jihun Blaber, Michael 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1219530110 <jats:p>A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 “prebiotic” α-amino acids. Before the emergence of biosynthetic pathways, this set is the most plausible resource for protein formation (i.e., proteogenesis) within the overall process of abiogenesis. An essential unsolved question regarding this prebiotic set is whether it defines a “foldable set”—that is, does it contain sufficient chemical information to permit cooperatively folding polypeptides? If so, what (if any) characteristic properties might such polypeptides exhibit? To investigate these questions, two “primitive” versions of an extant protein fold (the β-trefoil) were produced by top-down symmetric deconstruction, resulting in a reduced alphabet size of 12 or 13 amino acids and a percentage of prebiotic amino acids approaching 80%. These proteins show a substantial acidification of pI and require high salt concentrations for cooperative folding. The results suggest that the prebiotic amino acids do comprise a foldable set within the halophile environment.</jats:p> Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein Proceedings of the National Academy of Sciences |
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Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_unstemmed |
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_full |
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_fullStr |
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_full_unstemmed |
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_short |
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_sort |
simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
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Multidisciplinary |
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http://dx.doi.org/10.1073/pnas.1219530110 |
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2013 |
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2135-2139 |
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<jats:p>A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 “prebiotic” α-amino acids. Before the emergence of biosynthetic pathways, this set is the most plausible resource for protein formation (i.e., proteogenesis) within the overall process of abiogenesis. An essential unsolved question regarding this prebiotic set is whether it defines a “foldable set”—that is, does it contain sufficient chemical information to permit cooperatively folding polypeptides? If so, what (if any) characteristic properties might such polypeptides exhibit? To investigate these questions, two “primitive” versions of an extant protein fold (the β-trefoil) were produced by top-down symmetric deconstruction, resulting in a reduced alphabet size of 12 or 13 amino acids and a percentage of prebiotic amino acids approaching 80%. These proteins show a substantial acidification of pI and require high salt concentrations for cooperative folding. The results suggest that the prebiotic amino acids do comprise a foldable set within the halophile environment.</jats:p> |
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| author | Longo, Liam M., Lee, Jihun, Blaber, Michael |
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| description | <jats:p>A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 “prebiotic” α-amino acids. Before the emergence of biosynthetic pathways, this set is the most plausible resource for protein formation (i.e., proteogenesis) within the overall process of abiogenesis. An essential unsolved question regarding this prebiotic set is whether it defines a “foldable set”—that is, does it contain sufficient chemical information to permit cooperatively folding polypeptides? If so, what (if any) characteristic properties might such polypeptides exhibit? To investigate these questions, two “primitive” versions of an extant protein fold (the β-trefoil) were produced by top-down symmetric deconstruction, resulting in a reduced alphabet size of 12 or 13 amino acids and a percentage of prebiotic amino acids approaching 80%. These proteins show a substantial acidification of pI and require high salt concentrations for cooperative folding. The results suggest that the prebiotic amino acids do comprise a foldable set within the halophile environment.</jats:p> |
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| spelling | Longo, Liam M. Lee, Jihun Blaber, Michael 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.1219530110 <jats:p>A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 “prebiotic” α-amino acids. Before the emergence of biosynthetic pathways, this set is the most plausible resource for protein formation (i.e., proteogenesis) within the overall process of abiogenesis. An essential unsolved question regarding this prebiotic set is whether it defines a “foldable set”—that is, does it contain sufficient chemical information to permit cooperatively folding polypeptides? If so, what (if any) characteristic properties might such polypeptides exhibit? To investigate these questions, two “primitive” versions of an extant protein fold (the β-trefoil) were produced by top-down symmetric deconstruction, resulting in a reduced alphabet size of 12 or 13 amino acids and a percentage of prebiotic amino acids approaching 80%. These proteins show a substantial acidification of pI and require high salt concentrations for cooperative folding. The results suggest that the prebiotic amino acids do comprise a foldable set within the halophile environment.</jats:p> Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein Proceedings of the National Academy of Sciences |
| spellingShingle | Longo, Liam M., Lee, Jihun, Blaber, Michael, Proceedings of the National Academy of Sciences, Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein, Multidisciplinary |
| title | Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_full | Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_fullStr | Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_full_unstemmed | Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_short | Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_sort | simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| title_unstemmed | Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.1219530110 |