Production of a toxic polypeptide as a fusion inside GroEL cavity.The system is developed for efficient biosynthetic production of difficult-to-express polypeptides.  A target polypeptide is produced fused into T. thermophilus GroEL chaperonin polypeptide chain in such a way that it is presented inside the GroEL cavity near the substrate binding surface.  Thermostability of thermophilic GroEL can be used for its one-step separation from the host cell proteins by heating.  In this study, GroEL was adapted for methionine-specific cleavage with cyanogen bromide by total replacement of methionine residues to facilitate further purification of the target polypeptide. 
GroEL
Production of a toxic polypeptide as a fusion inside GroEL cavity.The system is developed for efficient biosynthetic production of difficult-to-express polypeptides.  A target polypeptide is produced fused into T. thermophilus GroEL chaperonin polypeptide chain in such a way that it is presented inside the GroEL cavity near the substrate binding surface.  Thermostability of thermophilic GroEL can be used for its one-step separation from the host cell proteins by heating.  In this study, GroEL was adapted for methionine-specific cleavage with cyanogen bromide by total replacement of methionine residues to facilitate further purification of the target polypeptide. 
GroEL
Production of a toxic polypeptide as a fusion inside GroEL cavity.The system is developed for efficient biosynthetic production of difficult-to-express polypeptides.  A target polypeptide is produced fused into T. thermophilus GroEL chaperonin polypeptide chain in such a way that it is presented inside the GroEL cavity near the substrate binding surface.  Thermostability of thermophilic GroEL can be used for its one-step separation from the host cell proteins by heating.  In this study, GroEL was adapted for methionine-specific cleavage with cyanogen bromide by total replacement of methionine residues to facilitate further purification of the target polypeptide. 
GroEL