Senisterra Guillermo A, Finerty Patrick J
Structural Genomics Consortium, Suite 700, 7th Floor, MaRS South Tower, 101 College St., Toronto, ON M51L7, Canada.
Mol Biosyst. 2009 Mar;5(3):217-23. doi: 10.1039/b814377c. Epub 2008 Dec 24.
The significant increase in the demand for purified protein for crystallization and structural studies has made necessary the development of multi-sample methods for identifying solution conditions that affect protein stability and aggregation. Conditions that stabilize proteins can improve protein purification and crystallization. These methods can be used to identify small molecule compounds or inhibitors that interact with the purified proteins, and might serve as starting points for drug discovery. In this article three methods for measuring protein stability and aggregation are described and discussed: differential scanning fluorimetry (DSF), differential static light scattering (DSLS), and isothermal denaturation (ITD).
用于结晶和结构研究的纯化蛋白质需求显著增加，因此有必要开发多种样品方法来确定影响蛋白质稳定性和聚集的溶液条件。稳定蛋白质的条件可改善蛋白质纯化和结晶。这些方法可用于识别与纯化蛋白质相互作用的小分子化合物或抑制剂，并可能作为药物发现的起点。本文描述并讨论了三种测量蛋白质稳定性和聚集的方法：差示扫描荧光法（DSF）、差示静态光散射法（DSLS）和等温变性法（ITD）。
