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Volumn 48, Issue 17, 2009, Pages 3708-3716

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

Author keywords

[No Author keywords available]

Indexed keywords

BACKBONE CARBONYL; BOUND WATERS; COVALENT MODIFICATIONS; CRYSTALLIN; ELECTRON TRANSFER; EXCITED-STATE ENERGY; EYE LENS; FAST ELECTRON TRANSFER; LENS PROTEINS; LENS TRANSPARENCY; NATIVE STATE; PHOTO-DAMAGE; PROTEIN COMPONENTS; PROTEIN DAMAGE; PROTEIN FOLDS; TRYPTOPHAN FLUORESCENCE; TRYPTOPHAN RESIDUES; UV RADIATION; UV RESISTANCE;

EID: 66049087099     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802177g     Document Type: Article
Times cited : (81)

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