Fig. 8From: Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modellingDistribution of the residues identified over SOD1 sequence. (1) Residues forming destructive hydrogen bonds, (2) residues from the interaction interface between copper-binding sites of both SOD1 monomers, (3) residues with top mean mechanical stiffness, (4) top evolutionarily conserved residues, (5) residues from contact between SOD1 aggregates, (6) schematic depiction of SOD1 secondary structure with indications of residues from copper-binding (pink triangles) and zinc-binding (gold triangles) sitesBack to article page