Protein design by directed evolution

被引:275
作者
Jaeckel, Christian [1 ]
Kast, Peter [1 ]
Hilvert, Donald [1 ]
机构
[1] ETH, Organ Chem Lab, CH-8093 Zurich, Switzerland
关键词
molecular diversity; random mutagenesis; screening; selection; enzymes; computational design;
D O I
10.1146/annurev.biophys.37.032807.125832
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
While nature evolved polypeptides over billions of years, protein design by evolutionary mimicry is progressing at a far more rapid pace. The mutation, selection, and amplification steps of the evolutionary cycle may be imitated in the laboratory using existing proteins, or molecules created de novo from random sequence space, as starting templates. However, the astronomically large number of possible polypeptide sequences remains an obstacle to identifying and isolating functionally interesting variants. Intelligently designed libraries and improved search techniques are consequently important for future advances. In this regard, combining experimental and computational methods holds particular promise for the creation of tailored protein receptors and catalysts for tasks unimagined by nature.
引用
收藏
页码:153 / 173
页数:21
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