Figure 1. SDS-PAGE of αBI5C and αBT162C mutant and wild-type αB-crystallins under different conditions. Lane 1 protein markers in kDa; lanes 2 and 5 show the wild-type αB-crystallin; lanes 3 and 6 show αBI5C; lanes 4 and 7 show αBT162C; lanes 2, 3, and 4 show proteins under reducing conditions; and lanes 5, 6, and 7 show proteins under non-reducing conditions. Both mutants form dimers under non-reducing conditions and the higher intensity of αBT162C dimer band than that of αBI5C dimer suggests that the COOH-terminal extensions in the subunits interact more compared to the interactions between NH₂-terminal regions.