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Mechanism of the Very Efficient Quenching of Tryptophan Fluorescence in Human γD- and γS-Crystallins: The γ-Crystallin Fold May Have Evolved To Protect Tryptophan Residues from Ultraviolet Photodamage
[Image: see text] Proteins exposed to UV radiation are subject to irreversible photodamage through covalent modification of tryptophans (Trps) and other UV-absorbing amino acids. Crystallins, the major protein components of the vertebrate eye lens that maintain lens transparency, are exposed to ambi...
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| Main Authors: | , , |
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| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
American Chemical Society
2009
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| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2674318/ https://ncbi.nlm.nih.gov/pubmed/19358562 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi802177g |
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