β-Crystallin is the most heterogeneous of the crystallin classes, with at least six different gene products, at least ten different post-translational modifications, and quaternary structure variants from dimers to octamers. However, all sequences are highly conserved through evolution.
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βL-Crystallin is one of the major lens proteins that aggregates under UV. A chaperone mixture of D-pathethine and N-acetyl carnosine has the ability to slow down the rate of photoaggregatin βL-Crystallin, and may be important in the prevention of cataract.
Journal of photochemistry and photobiology. B, Biology, 167, 15-19 (2017-01-01)
The damage produced by UV-C radiation (100-280nm) in organisms and cells is a well known fact. The main reactions of proteins to UV-C radiation consist in the alteration of their secondary structures, exposure of hydrophobic residues, unfolding and aggregation. Furthermore
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