Novel methods for directed evolution of enzymes: quality, not quantity.
In the past decade methods of directed molecular evolution have proven revolutionary in protein engineering. An increasing number of powerful new combinatorial techniques have joined rational design methods as effective tools for the manipulation and tailoring of biocatalysts. More and more, research in this maturing field is focusing on the quality and comprehensiveness of library construction and analysis. Additionally, in-depth studies have begun to highlight the underlying evolutionary mechanisms, limitations, and consequences of the various methodologies. Together, these investigations are creating a framework for future engineering projects.
Lutz
Stefan
S
Department of Chemistry, Emory University, 1515 Dickey Drive, Atlanta, Georgia 30322, USA. sal2@emory.edu
Patrick
Wayne M
WM
D000465:Algorithms; D001709:Biotechnology / Q000379:methods; D002384:Catalysis; D019020:Directed Molecular Evolution / Q000379:methods*; D015195:Drug Design; D004798:Enzymes / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics*; D019143:Evolution, Molecular; D020869:Gene Expression Profiling / Q000379:methods; D008957:Models, Genetic; D016297:Mutagenesis, Site-Directed / Q000235:genetics; D015202:Protein Engineering / Q000379:methods*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D020539:Sequence Analysis, Protein / Q000379:methods*
D004798:Enzymes; D011994:Recombinant Proteins