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Figure 3 | Microbial Cell Factories

Figure 3

From: Recombinant polypeptide production in E. coli: towards a rational approach to improve the yields of functional proteins

Figure 3

Characteristics of the recombinant protein aggregates. Recombinant polypeptides can aggregate in the inclusion bodies that are either completely inactive (a) or trap different amounts of active protein (b). Furthermore, the polypeptides can be released from the inclusion bodies and a network of chaperones and foldases/isomerases can convert misfolded constructs into native proteins (c). Highly soluble carriers fused to the target proteins can simplify the purification step (d) or keep in solution thermodynamically unfavorable partners for the time necessary to the folding machinery to complete its work (e). Nevertheless, the partner can finally fail to fold, remaining (partially) misfolded. Such misfolded domains exposing hydrophobic residues tend to form micelles that are kept in solution by the soluble carriers that constitute an external hydrophilic layer (f). Such soluble aggregates can be used to deliver the cargo in vivo and the carriers can be cleaved off when the biologically relevant target is reached.

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