Bai Yawen, Feng Hanqiao
Laboratory of Biochemistry, National Cancer Institute, NIH, Bethesda, MD 20892, USA.
Eur J Biochem. 2004 May;271(9):1609-14. doi: 10.1111/j.1432-1033.2004.04074.x.
To facilitate the process of protein design and learn the basic rules that control the structure and stability of proteins, combinatorial methods have been developed to select or screen proteins with desired properties from libraries of mutants. One such method uses phage-display and proteolysis to select stably folded proteins. This method does not rely on specific properties of proteins for selection. Therefore, in principle it can be applied to any protein. Since its first demonstration in 1998, the method has been used to create hyperthermophilic proteins, to evolve novel folded domains from a library generated by combinatorial shuffling of polypeptide segments and to convert a partially unfolded structure to a fully folded protein.
为了促进蛋白质设计过程并了解控制蛋白质结构和稳定性的基本规则，人们开发了组合方法，以便从突变体文库中选择或筛选具有所需特性的蛋白质。一种这样的方法利用噬菌体展示和蛋白水解来选择稳定折叠的蛋白质。该方法在选择时不依赖于蛋白质的特定特性。因此，原则上它可以应用于任何蛋白质。自1998年首次展示以来，该方法已被用于创建超嗜热蛋白质，从通过多肽片段组合改组产生的文库中进化出新的折叠结构域，并将部分未折叠的结构转化为完全折叠的蛋白质。
