Effect of mutations on the folding and stability of D-crystallin protein.

Interprotein interactions between the partially unfolded states of D-crystallin (D-crys) protein are known to cause cataracts. Therefore, understanding the unfolding pathways of native D-crys is extremely crucial to delineate their aggregation mechanism. In this study, we have performed extensive all-atom Molecular Dynamics simulations with explicit solvent to understand the role of the critical residues that drive the stability of the motifs and domains of D-crys in its wild type and mutant forms.