| Literature DB >> 15718133 |
Cintia Roodveldt1, Amir Aharoni, Dan S Tawfik.
Abstract
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.Entities:
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Year: 2005 PMID： 15718133 DOI： 10.1016/j.sbi.2005.01.001
Source DB: PubMed Journal: Curr Opin Struct Biol ISSN： 0959-440X Impact factor: 6.809