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Investigating and Engineering Enzymes by Genetic Selection
Author(s) -
Taylor Sean V.,
Kast Peter,
Hilvert Donald
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010917)40:18<3310::aid-anie3310>3.0.co;2-p
Subject(s) - directed molecular evolution , directed evolution , protein engineering , natural selection , selection (genetic algorithm) , computational biology , folding (dsp implementation) , darwinism , biochemical engineering , protein folding , mechanism (biology) , protein evolution , computer science , biology , synthetic biology , evolutionary biology , mutant , enzyme , genetics , machine learning , biochemistry , engineering , gene , physics , quantum mechanics , electrical engineering
Natural enzymes have arisen over millions of years by the gradual process of Darwinian evolution. The fundamental steps of evolution—mutation, selection, and amplification—can also be exploited in the laboratory to create and characterize protein catalysts on a human timescale. In vivo genetic selection strategies enable the exhaustive analysis of protein libraries with 10 10 different members, and even larger ensembles can be studied with in vitro methods. Evolutionary approaches can consequently yield statistically meaningful insight into the complex and often subtle interactions that influence protein folding, structure, and catalytic mechanism. Such methods are also being used increasingly as an adjunct to design, thus providing access to novel proteins with tailored catalytic activities and selectivities.