Fig. 6.

Comparison between γD (left) and βB1ΔN41 (right) crystallins. Panel a: tertiary structures embedded into solvent accessible area, generated by Schrödinger software⁶³. Panel b: charged amino acid residues on surfaces of proteins; positive – blue, negative – red, neutral – white. The location of residues is shown in the Hammer projection⁶⁴, having the polar and the azimuthal angles as the principle coordinate axes. An implementation of this projection was proposed by Koromyslova⁶⁵ et al and modified by us, as described in SI.