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PHOTOCHEMISTRY OF BIOLOGICAL MOLECULES – II. PHOTOLYSIS OF DIPEPTIDES IN THE SOLID STATE
Author(s) -
Johns R. B.,
Looney F. D.,
Whelan D. J.
Publication year - 1968
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1968.tb05830.x
Subject(s) - chemistry , photodissociation , radical , photochemistry , carbon atom , phenylalanine , molecule , nitrogen atom , peptide bond , double bond , peptide , amino acid , polymer chemistry , organic chemistry , ring (chemistry) , biochemistry
— Photolysis with light of 2537 Å of a series of aliphatic dipeptides in the solid state has been shown to lead to bond rupture and free radical formation. The structures of the radicals have been determined by ESR techniques and in general, the free electron has been shown to reside on the carbon atom attached to the nitrogen atom of the peptide bond. Dipeptides containing phenylalanine residues show ESR spectra typical of the free amino‐acid in the terminal position.