The folding landscape of an a-lytic protease variant reveals the role of a conserved b-hairpin in the development of kinetic stability
Most secreted bacterial proteases, including a-lytic protease (aLP), are synthesized with covalently attached pro regions necessary for their folding. The aLP folding landscape revealed that its pro region, a potent folding catalyst, is required to circumvent an extremely large folding free energy o...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2005-01, Vol.61 (1), p.105-114 |
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| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Online-Zugang: | Volltext |
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