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.
|Number of pages||7|
|Journal||Current Opinion in Structural Biology|
|Issue number||1 SPEC. ISS.|
|State||Published - 1 Jan 2005|
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology