期刊
ANNUAL REVIEW OF BIOPHYSICS
卷 37, 期 -, 页码 153-173出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev.biophys.37.032807.125832
关键词
molecular diversity; random mutagenesis; screening; selection; enzymes; computational design
类别
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据