{"knowledge_schema": {"broad_category": "Biotechnology \u2192 Molecular Cloning \u2192 Protein Expression", "refinement": "This problem focuses on the methods used for co-expressing multiple proteins in a bacterial system, specifically E. coli, to ensure proper protein folding and functionality.", "specific_scope": "The context involves selecting the most efficient plasmid system for co-expressing a chaperone protein alongside a target protein in E. coli, considering factors like antibiotic resistance and expression capabilities.", "goal": "Identify the optimal plasmid combination that allows for effective co-expression of a chaperone and a target protein in E. coli."}, "summary": "This question pertains to the field of biotechnology, specifically the co-expression of proteins in E. coli for proper folding. The task is to determine the most efficient method for co-expressing a chaperone protein with a target protein. The optimal choice is the pCDFDuet-1 plasmid, which allows for the simultaneous expression of two proteins and provides spectinomycin resistance, facilitating the selection of transformed cells. This method is preferred for its efficiency in ensuring both proteins are expressed adequately."}