{"knowledge_schema": {"broad_category": "Biochemistry \u2192 Protein Interactions \u2192 Post-Translational Modifications", "refinement": "This problem involves analyzing the effects of phosphorylation on protein interactions and complex formations among recombinant mammalian proteins.", "specific_scope": "The focus is on understanding how phosphorylation of protein A influences its interactions with other proteins (B, C, D) and the resulting complexes formed under different experimental conditions.", "goal": "Determine the impact of phosphorylation on protein A's interactions and the resulting protein complexes based on SEC-MALS data."}, "summary": "This problem examines the effects of phosphorylation on the interactions between four recombinant mammalian proteins. The data from various experiments indicate how these proteins behave under different conditions, particularly focusing on the role of phosphorylation of protein A. The goal is to understand how this modification affects protein A's affinity for other proteins and the formation of complexes. The conclusion drawn is that phosphorylation of protein A decreases its affinity to one of the proteins (B, C, or D), and that protein A exists predominantly as a homodimer."}