Directed evolution of proteins for heterologous expression and stability.
Curr Opin Struct Biol
; 15(1): 50-6, 2005 Feb.
Article
en En
| MEDLINE
| ID: mdl-15718133
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.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
/
Ingeniería de Proteínas
/
Proteínas
/
Regulación de la Expresión Génica
/
Evolución Molecular Dirigida
/
Escherichia coli
Idioma:
En
Revista:
Curr Opin Struct Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2005
Tipo del documento:
Article
País de afiliación:
Israel