{"knowledge_schema": {"broad_category": "Biochemistry \u2192 Protein Structure and Function \u2192 Membrane Proteins", "refinement": "This problem focuses on the effects of different detergents on the oligomeric state of a membrane protein during purification and analysis.", "specific_scope": "The context involves comparing the mass spectrometry results of the mitochondrial membrane protein Kag2 when purified with two different detergents, DDM and Triton X-100.", "goal": "To infer the oligomeric state of Kag2 based on the mass spectrometry data obtained from different detergent treatments."}, "summary": "This problem involves understanding how different detergents affect the oligomeric state of a membrane protein, Kag2. The mass spectrometry results indicate that when purified with DDM, Kag2 appears as a larger complex (105000 Da), suggesting it is stabilized in a trimeric form. In contrast, Triton X-100 results in a mass corresponding to the monomeric state (35000 Da). Therefore, the inference is that DDM stabilizes a trimeric form of Kag2, while Triton X-100 does not promote oligomerization."}