While it is expected that partly unfolded proteins expose some hydrophobic surfaces, and such hydrophobic regions exist in SOD1,44 it could not be anticipated that diverse ALS-causing SOD1 point mutations, causing a variety of alterations on the properties of the proteins, all increase the propensity to expose hydrophobic surfaces and that this common feature is the molecular determinant underlying the formation of the ordered aggregates. Here, SOD1 is linked to amyotrophic lateral sclerosis.