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 …

Formation of inclusion bodies in bacterial hosts poses a major challenge for large scale
recovery of bioactive proteins. The process of obtaining bioactive protein from inclusion …

During the proteomics period, the growth in the use of recombinant proteins has increased
greatly in the recent years. Bacterial systems remain most attractive due to low cost, high …

Protein-protein interaction (PPI) is a hot topic in clinical research as protein networking has a
major impact in human disease. Such PPIs are potential drugs targets, leading to the need …

The stability of proteins in aqueous solution is routinely enhanced by cosolvents such as
glycerol. Glycerol is known to shift the native protein ensemble to more compact states …

Motivation: Protein insolubility is a major obstacle for many experimental studies. A
sequence-based prediction method able to accurately predict the propensity of a protein to …

Highlights•The need for recombinant proteins both as biopharmaceuticals and for structural
studies in drug development is outlined.•The basis of the production of recombinant proteins …

Recombinant proteins expressed as bacterial inclusion bodies (IBs) are now receiving
tremendous attention for many diverse applications in the areas of industrial and medical …

Almost all of the 200 or so approved biopharmaceuticals have been produced in one of
three host systems: the bacterium Escherichia coli, yeasts (Saccharomyces cerevisiae …

This chapter describes the use of glutathione S-transferase (GST) gene fusion proteins as a
method for inducible, high-level protein expression and purification from bacterial cell …