Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 13, Issue 1, Pages 26-34Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2009.02.021
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Funding
- Czech Ministry of Education [LC06010, MSM0021622412, MSM0021622413]
- Czech Science Foundation [201/07/0927, 203/08/0114]
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Current computational tools to assist experimentalists for the design and engineering of proteins with desired catalytic properties are reviewed. The applications of these tools for de novo design of protein active sites, optimization of substrate access and product exit pathways, redesign of protein-protein interfaces, identification of neutral/advantageous/deleterious mutations in the libraries from directed evolution and stabilization of protein structures are described. Remarkable progress is seen in de novo design of enzymes catalyzing a chemical reaction for which a natural biocatalyst does not exist. Yet, constructed biocatalysts do not match natural enzymes in their efficiency, suggesting that more research is needed to capture all the important features of natural biocatalysts in theoretical designs.
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