Sandberg W S, Terwilliger T C
Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.
Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8367-71. doi: 10.1073/pnas.90.18.8367.
A method for simultaneously engineering multiple properties of a protein, based on the observed additivity of effects of individual mutations, is presented. We show that, for the gene V protein of bacteriophage f1, effects of double mutations on both protein stability and DNA binding affinity are approximately equal to the sums of the effects of the constituent single mutations. This additivity of effects implies that it is possible to deliberately construct mutant proteins optimized for multiple properties by combination of appropriate single mutations chosen from a characterized library.
基于观察到的单个突变效应的可加性，本文提出了一种同时改造蛋白质多种特性的方法。我们表明，对于噬菌体f1的基因V蛋白，双突变对蛋白质稳定性和DNA结合亲和力的影响大致等于组成单突变效应的总和。这种效应的可加性意味着，可以通过从一个已表征的文库中选择合适的单突变进行组合，来特意构建针对多种特性进行优化的突变蛋白。
