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- W2050591106 abstract "1. Tyr-72 is included in the hydrophobic cleft which is formed in the histone H1 globular head. 2. Tyr-72 is screened against polar aqueoys environment and its intramolecular mobility is sharply retarded. 3. This microenvironment causes a red shift (λmax = 279 nm) and a sharpening of the longer wavelength shoulder of absorption spectra, a high fluorescence anisotropy value (A = 0,11), high quantum yield of fluorescence (∼0.2) and a decrease of the Stern-Volmer constant during quenching of histone H1 fluorescence by acrylamide. 4. It has been found that the change in the intensity of histone fluorescence at λexcit = 265 nm, but not at λexcit = 280 nm, is due to the changes in the quantum yield of fluorescence. 5. The increase of fluorescence intensity at λexcit = 280 nm depends on the changes in the quantum yield and molar extinction coefficient of histone H1 tyrosyl chromophore. 6. The change in the ratio of fluorescence intensity exited at 280 nm (F280) to the fluorescence intensity excited at 265 nm (F265) corresponds to the change of Δ ϵ286 in difference absorption spectra. 7. The introduction of the parameter Cf = F280F265 allows one to go over to studying excitation spectrum shifts instead of histone absorption spectrum shifts, which is much more convenient methodologically since in this case it is possible to carry out research using lower protein concentrations and turbid solutions. 8. The results make it possible to designate Tyr-72 of histone H1 as a special class of fluorescent tyrosyls whose properties differ from those of tyrosyls of other tryptophane-free proteins: RNAase, insulin, core histones — H2A, H2B, H3, H4 and some others." @default.
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- W2050591106 date "1985-01-01" @default.
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- W2050591106 title "Intrinsic fluorescence, difference spectrophotometry and theoretical studies on tertiary structure of calf thymus histone H1" @default.
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- W2050591106 doi "https://doi.org/10.1016/0020-711x(85)90117-x" @default.
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