Solubility of Thaumatin
| Autor: | Sarah Knafo, Neer Asherie, Charles Ginsberg, Arieh Greenbaum, Samuel Blass |
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| Rok vydání: | 2008 |
| Předmět: | |
| Zdroj: | Crystal Growth & Design. 8:1815-1817 |
| ISSN: | 1528-7505 1528-7483 |
| DOI: | 10.1021/cg800276r |
| Popis: | Thaumatin, an intensely sweet protein, crystallizes rapidly in the presence of tartrate ions. The ease with which crystals form has led to the use of thaumatin over the past decade as a model system for the study of protein crystallization. The available data on the solubility of this protein, however, are inconsistent. We have purified thaumatin and determined its solubility with the l and d enantiomers of the tartrate ion. We find that the crystal habit and solubility are significantly different for the two precipitants: the solubility increases with temperature in l-tartrate, while it decreases with temperature in d-tartrate. Our results suggest that the chirality of precipitants is an important factor that should be controlled when determining the solubility of proteins. |
| Databáze: | OpenAIRE |
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