Tryptophan oxidation-induced dynamics highlight why stable γS-crystallin variants aggregate.
These findings support the established model in which crystallin aggregation is decoupled from global destabilization: although the oxidative modification at W163 is structurally tolerated through rearrangement of the local hydrogen bond network, the resulting changes in backbone flexibility render aggregation-competen...
Yeonseong Seo, Amanda Abiad, Micco Iwase et al.
· Biophysics Reports · 0 citations