{"knowledge_schema": {"broad_category": "Biochemistry \u2192 Protein Structure \u2192 Protein-Protein Interactions", "refinement": "This problem focuses on the types of interactions that stabilize protein dimers, specifically non-covalent interactions.", "specific_scope": "The context involves analyzing the dimerization interface of Protein XER22 to determine the predominant interactions responsible for its stable dimer formation.", "goal": "Identify the type of non-covalent interactions that contribute to the stability of the dimer formed by Protein XER22."}, "summary": "This problem examines the non-covalent interactions that stabilize the dimerization of Protein XER22. The dimerization interface sequence suggests that hydrophobic interactions are the most likely contributors to the stability of the dimer, as these interactions typically play a crucial role in protein-protein interactions. The goal is to understand the nature of these interactions to explain how the dimer is formed and maintained."}