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EXCITATION‐ENERGY TRANSFER BETWEEN TYROSINE AND TRYPTOPHAN IN PROTEINS EVALUATED BY THE SIMULTANEOUS MEASUREMENT OF FLUORESCENCE AND ABSORBANCE
Author(s) -
Saito Yoshio,
Tachibana Hideki,
Hayashi Hidechika,
Wada Akiyoshi
Publication year - 1981
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.1751-1097.1981.tb05420.x
Subject(s) - absorbance , fluorescence , chemistry , tryptophan , quantum yield , globular protein , tyrosine , analytical chemistry (journal) , excitation , energy transfer , wavelength , excitation wavelength , yield (engineering) , photochemistry , chromatography , chemical physics , amino acid , optics , crystallography , thermodynamics , biochemistry , physics , quantum mechanics
— The efficiencies of the excitation–energy transfer from tyrosine to tryptophan residues in eight globular proteins in the native and denatured states are obtained by studying the wavelength dependence of the fluorescence quantum yield. The measurements are made over a wide wavelength range using a computer‐controlled spectrophotometer which can measure the fluorescence and absorbance simultaneously in one sample solution (Wada et al. , 1980). The values of the energy transfer efficiencies ranged from 0.17 ± 0.12 to 0.69 ± 0.06 in the native state and from ‐0.04 ± 0.09 to 0.12 ± 0.06 in the denatured state. These values are considerably lower than the values reported by Kronman and Holmes (1971); in particular, an almost complete absence of energy transfer for the denatured state is shown.