Accumulative deamidation of human lens protein γS-crystallin leads to partially unfolded intermediates with enhanced aggregation propensity
C. J. Vetter, D. Thorn, S. G. Wheeler, C. Mundorff, K. Halverson-Kolkind, J. A. Carver, L. L. David, K. J. Lampi
This study shows that deamidation of γS-crystallin at specific sites leads to protein destabilization, increased unfolding, and enhanced aggregation in cataractous lenses.
bioRxiv · Feb 21, 2020 · PreprintBiochemistry