Nearly 30% of currently approved recombinant therapeutic proteins are produced in
Escherichia coli. Due to its well-characterized genetics, rapid growth and high-yield …

Bacteria are simple and cost effective hosts for producing recombinant proteins. However,
their physiological features may limit their use for obtaining in native form proteins of some …

Many heterologous polypeptides fail to fold into their native state when expressed in
Escherichia coli; instead, they are either degraded by the cellular proteolytic machinery or …

The high-level expression of recombinant gene products in the gramnegative bacterium
Escherichia coli often results in the misfolding of the protein of interest and its subsequent …

PreS2-S′-β-galactosidase, a three-domain fusion protein that aggregates extensively in the
cytoplasm of Escherichia coli, was used to systematically investigate the effects of heat …

Disulfide bonds are normally formed after a polypeptide has been exported from the
reducing environment of the cytoplasm into a more oxidizing compartment, such as the …

Extracellular production of heterologous proteins using the Escherichia coli cell factory offers
several advantages over intracellular production and mammalian culture. Properly folded …

US6335160B1 - Methods and compositions for polypeptide engineering - Google Patents
US6335160B1 - Methods and compositions for polypeptide engineering - Google Patents …

US6303344B1 - Methods and compositions for polypeptide engineering - Google Patents
US6303344B1 - Methods and compositions for polypeptide engineering - Google Patents …

US6946296B2 - Methods and compositions for polypeptide engineering - Google Patents
US6946296B2 - Methods and compositions for polypeptide engineering - Google Patents …