Summary
The photosensitivity of cystine and the aromatic amino acids tryptophan, tyrosine and phenylalanine in different proteins, in aqueous solution and in the adsorbed (solid) state is compared with the photosensitivity of these amino acids in thermal polymers ofα-amino acids. The photosensitivity of cystine in the absence of chromophoric groups is largely independent of the amino acid composition, primary structure, or conformation of the polymer. The interaction between the “sensitizer” (aromatic amino acid residues), and cystine, however, is largely dependent on the conformation of the polymer if energy or charge transfer is involved. The effects of tryptophan photolysis products (solvated electrons) appear to be largely independent of the conformational state.
Zusammenfassung
Die Photosensibilität des Cystins und der aromatischenAminosäuren Tryptophan, Tyrosin and Phenylalanin in verschiedenen Proteinen, in wäßriger Lösung und in adsorbiertem Zustand wurde mit der Photoempfindlichkeit dieser Aminosäuren in thermischen Polymeren von Aminosäuren verglichen. In Abwesenheit von chromophoren Gruppen ist die Photosensibilität des Cystins weitgehend unabhängig von Aminosäurezusammensetzung, Primärstruktur oder Konformation des Polymeren. Die Wechselwirkung zwischen „Sensibilisator“ (meist aromatischen Aminosäuren) und Cystin ist nur konformationsabhängig, wenn Energie- oder Charge-Transferprozesse beteiligt sind. Die Wirkung der Photolyseprodukte des Tryptophans (solvatisierter Elektronen) scheint dagegen weitgehend unabhängig von der Konformation zu sein.
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Dose, K., Brand, M.C. Zur Abhängigkeit der Photosensibilität von Aminosäuren von Umgebungsfaktoren. Biophysik 7, 140–145 (1971). https://doi.org/10.1007/BF01190147
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DOI: https://doi.org/10.1007/BF01190147