Directed evolution of proteins for heterologous expression and stability

Cintia Roodveldt, Amir Aharoni, Dan S. Tawfik

Research output: Contribution to journalReview articlepeer-review

124 Scopus citations


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.

Original languageEnglish
Pages (from-to)50-56
Number of pages7
JournalCurrent Opinion in Structural Biology
Issue number1 SPEC. ISS.
StatePublished - 1 Jan 2005
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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