Solubility of thaumatin
Solubility of thaumatin
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DOI：
10.1021/cg800276r
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发表时间：
2008-06-01
影响因子：
3.8
通讯作者：
Knafo, Sarah
中科院分区：
文献类型：
--
作者：
Asherie, Neer;Ginsberg, Charles;Knafo, Sarah
奇异果甜蛋白是一种非常甜的蛋白质，在酒石酸盐离子存在下迅速结晶。在过去的十年里，由于晶体形成的容易性，索马甜被用作研究蛋白质结晶的模型系统。然而，关于这种蛋白质的溶解度的可用数据是不一致的。我们已经纯化了索马甜，并确定了其与酒石酸根离子的L和D对映体的溶解度。我们发现两种沉淀剂的结晶习性和溶解度有显著的不同：在L-酒石酸盐中溶解度随温度的升高而增加，而在D-酒石酸盐中溶解度随温度的升高而降低。我们的研究结果表明，沉淀剂的手性是一个重要的因素，应控制时，确定蛋白质的溶解度。
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.