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• W1601647590 startingPage "369" @default.
• W1601647590 abstract "Abstract 1. 1.|Peptide bonds and aliphatic amino acid constituents have been considered to be of minor significance in accounting for light damage in proteins. A representative group of aliphatic amino acids has now been shown to be sensitive to ultraviolet light and to form free radicals on irradiation. 2. 2.|Polycrystalline samples of l -alanine, dl -valine, dl -aminoisobutyric acid, dl -isoleucine, dl -α- amino -n- butyric and -n-valeric acids, glycine and suitably N-deuterated and carbon-deuterated derivatives have been photolysed. The structures of the radicals have been deduced from electron spin resonance spectral data and, in general, are the result of deamination reactions. 3. 3.| l -Tyrosine, and dl -tryptophan were also photolysed and formed radicals of undetermined structure. l -Phenylalanine was also damaged by ultraviolet light and the electron spin resonance spectrum suggested one radical which gave no observable hyperfine structure together with a second radical interpreted as possessing a cyclohexadienyl-type structure resulting from H-atom addition to the benzenoid ring. A similar radical was observed from photolysed glycyl- dl -phenylalanine." @default.
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• W1601647590 date "1967-10-23" @default.
• W1601647590 modified "2023-10-07" @default.
• W1601647590 title "Photochemistry of biological molecules. I. Photolysis of amino acids in the solid state." @default.
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