An Internal Disulfide Locks A Misfolded Aggregation-Prone Intermediate In Cataract-Linked Mutants Of Human Gamma-D Crystallin
BIOPHYSICAL JOURNAL(2017)
Abstract
A large class of non-amyloid protein aggregates are considered amorphous; in most cases little is known about detailed mechanisms, if any, that underlie these aggregation phenomena. Amorphous aggregation of the γ-crystallins in the eye lens causes a widespread disease of aging, cataract. We combined simulations and experiments to study the mechanism of aggregation of two γD-crystallin mutants, the congenital cataract mutation W42R and the mimic of age-related oxidative damage W42Q. The two mutants had highly similar properties.
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Key words
cataract,crystallin,disulfide,oxidative stress,protein aggregation,protein misfolding,all-atom Monte Carlo simulation,domain swapping,unfolding intermediate
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