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• W1555806704 abstract "1.|Compounds were synthesized as models for quenching of tryptophan and tyrosine fluorescence in proteins. Bis-indole-3-methylene disulfide, bis-4-methoxybenzyl disulfide and their corresponding reduced, sulfhydryl derivatives were of extremely low fluorescence. The loss of fluorescence is ascribed to internal quenching by the disulfide and sulfhydryl groups. 2.|Similar results were obtained for l-cystinyl-bis-l-tyrosine, HOOC(CH2)2-S-S-Cys-Tyr, ribonuclease-(SCH2CH2COOH)8, and their reduced or carboxy-methylated products. That is, the disulfide group strongly quenched the fluorescence; the reduced sulfhydryl group quenched less. 3.|The mechanism of quenching has not been established but several of the common pathways were rejected. The most probable mechanism seems to be an extremely short-range interaction between the aromatic ring and the sulfur atoms that facilitates a vibrational dissipation of the excitation energy." @default.
• W1555806704 created "2016-06-24" @default.
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• W1555806704 date "1967-05-01" @default.
• W1555806704 modified "2023-10-02" @default.
• W1555806704 title "Fluorescence and protein structure" @default.
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• W1555806704 doi "https://doi.org/10.1016/0005-2795(67)90379-0" @default.
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