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- W2079015998 abstract "Fluorimetric titration data are presented for tyrosyl peptides, insulin and native RNAase. Equations were derived to fit these data, and the following conclusions were drawn: 1. Changes in fluorescence of simple tyrosyl peptides are explicable in terms of changes in the ionic state of the phenolic and neighboring amino groups. 2. Ionized phenolic groups of molecules with multiple tyrosyl residues appear to function as sinks for loss of fluorescent energy of the molecule. 3. Fluorimetric titration data of native RNAase can be accounted for with reasonable accuracy by subdivision of the six tyrosyl residues into three normal residues that are strongly fluorescent (5·5% quantum efficiency) and three abnormal residues that are non-fluorescent or virtually so (less than 0.2% quantum efficiency). 4. Abnormal tyrosyl residues of native RNAase appear to serve as rather inefficient sinks for loss of fluorescence, even at neutral pH." @default.
- W2079015998 created "2016-06-24" @default.
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- W2079015998 date "1965-01-01" @default.
- W2079015998 modified "2023-09-27" @default.
- W2079015998 title "Fluorescence and the structure of proteins V. Ionization of tyrosyl residues" @default.
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- W2079015998 doi "https://doi.org/10.1016/0926-6585(65)90010-5" @default.
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