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Curr Opin Struct Biol. 2005 Feb;15(1):50-6.

Directed evolution of proteins for heterologous expression and stability.

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  • 1Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.


Recent developments have been made in the application of directed evolution to achieve the efficient heterologous expression of proteins in Escherichia coli and yeast by increasing the stability and solubility of the protein in the host environment. One interesting conclusion that emerges is that the evolutionary process often improves the stability and solubility of an intermediate (apoprotein, proprotein or folding intermediate) that otherwise constitutes a bottleneck to functional expression, rather than altering the protein's final state.

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