溶菌酶在硝酸乙基铵/水混合溶剂中的溶解度和一种新的蛋白质结晶方法。
The solubility of hen lysozyme in ethylammonium nitrate/H2O mixtures and a novel approach to protein crystallization.
机构信息
Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA.
出版信息
Molecules. 2010 Feb 4;15(2):793-803. doi: 10.3390/molecules15020793.
We report on the solubility of hen lysozyme (HEWL) in aqueous ethylammonium nitrate (EAN) as a function of water content. We find the solubility behavior to be complex, exhibiting both a maximum (400 mg/mL) at very high EAN content) and a minimum at intermediate EAN content. We exploit this solubility profile in a novel approach to generating crystals of hydrophilic proteins, based on rehydration of a high concentration protein solution. We describe the production of crystals of X-ray diffraction quality. Two related ionic liquid solvent systems, with the same solubility profiles but different effective pH characteristics, are identified for future evaluation.
我们报告了在水合乙基硝酸铵（EAN）中的鸡溶菌酶（HEWL）的溶解度作为含水量的函数。我们发现溶解度行为非常复杂，在非常高的 EAN 含量下（400mg/mL）存在最大值，而在中间 EAN 含量下存在最小值。我们利用这种溶解度曲线，通过再水合高浓度蛋白质溶液的新方法来生成亲水性蛋白质的晶体。我们描述了具有 X 射线衍射质量的晶体的产生。两种具有相同溶解度曲线但具有不同有效 pH 特性的相关离子液体溶剂系统已被确定用于进一步评估。
Zotero 插件