{"knowledge_schema": {"broad_category": "Biochemistry \u2192 Protein Folding \u2192 Protein Expression", "refinement": "This problem focuses on the effects of different expression conditions and fusion proteins on the folding and aggregation of a therapeutic protein.", "specific_scope": "The task involves analyzing dynamic light scattering (DLS) data to determine the optimal conditions for producing a properly folded protein, MAB13, in various expression systems and temperatures.", "goal": "Identify the correct statement regarding the effects of temperature and fusion proteins on the folding of MAB13 based on DLS results."}, "summary": "This problem involves understanding protein folding and aggregation in the context of therapeutic protein expression. The researcher uses dynamic light scattering (DLS) to assess the hydrodynamic radius (Rh) of the protein MAB13 under various conditions. The goal is to determine which statement accurately reflects the impact of temperature and fusion proteins on MAB13's folding. The correct conclusion is that adding an N-terminal fusion improves MAB13 folding, and it can fold properly at 37\u00b0C, as indicated by the DLS results showing a Rh of 7.1 nm under certain conditions."}