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Nathaniel Schafheimer and Jonathan King Tryptophan Cluster Protects Human γD-Crystallin from Ultraviolet Radiation-Induced Photoaggregation In Vitro Photochemistry and Photobiology 89

Article first published online: 20 JUN 2013 | DOI: 10.1111/php.12096

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The Trp residues of human γD-crystallin (HγD-Crys) are highly conserved, and the energy transfer mechanism observed between them has been postulated to play a photoprotective role in this long lived, chronically ultraviolet radiation (UVR) exposed lens protein. Here, we see that replacement of the Trp's with Phe, while reducing HγD-Crys's absorbing capacity, increases the rate of protein photoaggregation, suggesting that the placement and orientation of the Trp's is an evolved protective structure that could aid in filtering harmful UVR to protect the retina.

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