Directed evolution of proteins for heterologous expression and stability

被引：104

作者：

Roodveldt, C ^{[1
]}

Aharoni, A ^{[1
]}

Tawfik, DS ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2005年 / 15卷 / 01期

基金：

以色列科学基金会;

关键词：

D O I：

10.1016/j.sbi.2005.01.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recent developments have been made in the application of directed evolution to achieve the efficient heterologous expression of proteins in Escherichia coli and yeast by increasing the stability and solubility of the protein in the host environment. One interesting conclusion that emerges is that the evolutionary process often improves the stability and solubility of an intermediate (apoprotein, proprotein or folding intermediate) that otherwise constitutes a bottleneck to functional expression, rather than altering the protein's final state.

引用

页码：50 / 56

页数：7