title: Directed evolution of proteins for heterologous expression and stability.
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.
authors.affiliation: Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Cintia
authors.initials: C
authors.lastname: Roodveldt
authors.forename: Amir
authors.initials: A
authors.lastname: Aharoni
authors.forename: Dan S
authors.initials: DS
authors.lastname: Tawfik
mesh_terms: D003001:Cloning, Molecular / Q000379:methods; D019020:Directed Molecular Evolution / Q000379:methods*; D004926:Escherichia coli / Q000502:physiology*; D019143:Evolution, Molecular; D005786:Gene Expression Regulation / Q000502:physiology*; D024861:Genetic Enhancement / Q000379:methods; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis; D012441:Saccharomyces cerevisiae / Q000502:physiology*; D012995:Solubility
chemical_list: D011506:Proteins; D011994:Recombinant Proteins