Escherichia coli is one of the most widely used hosts for the production of heterologous
proteins and its genetics are far better characterized than those of any other microorganism …

Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding
aggregates. Substantial data support the hypothesis that partially folded intermediates are …

E. coli is most preferred system used for the production of recombinant proteins in bacteria
and the availability of improved genetic tools/methods are making it more valuable than …

Protein aggregation is an ordinary consequence of thermal stress. In recombinant bacteria,
the over-expression of plasmid-encoded genes triggers transcription of heat-shock genes …

A common limitation of recombinant protein production in bacteria is the formation of
insoluble protein aggregates known as inclusion bodies. The propensity of a given protein to …

Background The overproduction of recombinant proteins in host cells often leads to their
misfolding and aggregation. Previous attempts to increase the solubility of recombinant …

The efficient in vivo folding of many heterologous proteins is a major bottleneck of high level
production in bacterial hosts and simple optimisation protocols have not been available yet …

Expression of recombinant proteins in Escherichia coli (E. coli) remains the most popular
and cost-effective method for producing proteins in basic research and for pharmaceutical …

High-throughput protein expression and purification has a central, pivotal role in structural
genomics. In fact, crystallographic-quality protein production on the scale required to …

Bacterial inclusion bodies (IBs) are refractile aggregates of protease-resistant misfolded
protein that often occur in recombinant bacteria upon gratuitous overexpression of cloned …