[Spectroscopy of intermolecular interactions of a tyrosine chromophore. III. Classification of the state of tyrosine residues in proteins based on their electron spectra].
Absorption and fluorescence spectra of some tyrosine-containing proteins were analysed. Comparison of the peculiarities of fluorescence and absorption of the tyrosine chromophore in the model compounds and proteins suggested a new classification of the states of tyrosine residues in proteins: I -- tyrosyls with hydrated OH-group (lambda mf approximately equal to 304 nm); II -- tyrosyls, whose hydroxyl group forms the hydrogen bond inside the protein in a hydrophobic surrounding or in the globular fold in structured water layer (lambda mf = 306-307 nm); III -- tyrosyls whose OH-group is deprotonated in the excited state (lambda mf approximately equal to 330-350 nm).
S N
SN
Krapunov
A I
AI
Dragan
D011506:Proteins / Q000032:analysis*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D014443:Tyrosine / Q000032:analysis*
D011506:Proteins; D014443:Tyrosine
Spektroskopiia mezhmolekuliarnykh vzaimodeĭstviĭ tirozinovogo khromofora. III. Klassifikatsiia sostoianiia ostatkov tirozina v belkakh po ikh élektronnym spektram.