The Solubility of Hen Lysozyme in Ethylammonium Nitrate/H2O Mixtures and a Novel Approach to Protein Crystallization

被引：36

作者：

Byrne, Nolene ^{[1
]}

Angell, C. Austen ^{[1
]}

机构：

[1] Arizona State Univ, Dept Chem & Biochem, Tempe, AZ 85287 USA

来源：

MOLECULES | 2010年 / 15卷 / 02期

基金：

美国国家科学基金会;

关键词：

protic ionic liquids; protein crystallization; solubility and protein stability; IONIC LIQUIDS; STABILIZATION;

D O I：

10.3390/molecules15020793

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

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.

引用

页码：793 / 803

页数：11

共 28 条

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[2]

Bergfors T.M., 1999, Protein Crystallization: Techniques, Strategies, and Tips: A Labo- ratory Manual

[3]

Protein unfolding, and the "Tuning In" of reversible intermediate states, in protic ionic liquid media [J].