Engineering by homologous recombination: exploring sequence and function within a conserved fold

被引：39

作者：

Carbone, Martina N. ^{[1
]}

Arnold, Frances H. ^{[1
]}

机构：

[1] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2007年 / 17卷 / 04期

关键词：

D O I：

10.1016/j.sbi.2007.08.005

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：

In nature similar protein folds accommodate distant sequences and support diverse functions. This observation coupled with the recognition that proteins can tolerate many homologous substitutions inspires protein engineers to use recombination to search for new functions within sequences encoding structurally related molecules. These searches have led to proteins with novel activities, diversified specificities and greater stabilities. Computational methods that exploit structural and evolutionary information are being used to design highly mutated yet still natively folded chimeric proteins and protein libraries.

引用

页码：454 / 459

页数：6

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