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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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Autori principali: Chen, Jiejin, Callis, Patrik R., King, Jonathan
Natura: Artigo
Lingua:Inglês
Pubblicazione: American Chemical Society 2009
Accesso online: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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