Cataract-associated deamidations on the surface of γS-crystallin increase protein unfolding and flexibility at distant regions
H. M. Forsythe, C. J. Vetter, K. J. Jara, P. N. Reardon, L. L. David, E. J. Barbar, K. Lampi
This study identifies deamidation sites in γS-crystallin that increase protein dynamics and flexibility in distant regions, contributing to cataract formation.
bioRxiv · May 22, 2019 · PreprintBiophysics