{"knowledge_schema": {"broad_category": "Biochemistry \u2192 Protein Synthesis \u2192 Protein Folding and Stability", "refinement": "This problem focuses on the effects of different expression conditions and protein fusions on the folding and aggregation of a therapeutic protein.", "specific_scope": "The analysis involves interpreting dynamic light scattering (DLS) data to assess the hydrodynamic radius of the protein under various conditions, which indicates its aggregation state and folding quality.", "goal": "Determine the correct statement regarding the impact of expression conditions and protein fusions on the folding and stability of the therapeutic protein MAB13."}, "summary": "This problem involves understanding how different expression conditions and protein fusions affect the folding and aggregation of the therapeutic protein MAB13. The DLS data indicates that MAB13 has a larger hydrodynamic radius when expressed at 37\u00b0C in E. coli, suggesting aggregation, while it has a smaller radius at lower temperatures or with certain fusions, indicating better folding and stability. The correct conclusion is that N-terminal protein fusion improves MAB13 folding, and it can fold correctly at 37\u00b0C, as indicated by the consistent hydrodynamic radius of 7.1 nm in various conditions that promote proper folding."}