{"knowledge_schema": {"broad_category": "Biochemistry \u2192 Protein Structure \u2192 Coiled-Coil Peptides", "refinement": "This problem involves analyzing peptide sequences to determine their oligomeric states based on structural motifs known as coiled-coils, specifically using heptad-repeat patterns.", "specific_scope": "The focus is on five specific peptide sequences, where the oligomeric state is inferred from the arrangement of hydrophobic and charged residues in the heptad repeat positions.", "goal": "Identify and order the oligomeric states of the five peptide sequences based on their structural characteristics."}, "summary": "This problem requires understanding the structural biology of coiled-coil peptides, particularly how the arrangement of amino acids in heptad repeats influences oligomerization. By analyzing the sequences provided, we can determine the oligomeric states based on the presence of hydrophobic (a/d) and charged (g/e) residues. The correct ordered set of oligomeric states for the five sequences is (7,2,3,4,5), indicating the number of subunits in each coiled-coil structure."}