scholarly journals The thermodynamic characteristic of four-heme cytochrome c in Rhodopseudomonas viridis reaction centers, as derived from a quantitative analysis of the differential absorption spectra in α-domain

FEBS Letters ◽  
1990 ◽  
Vol 261 (1) ◽  
pp. 11-13 ◽  
Author(s):  
V.P. Shinkarev ◽  
A.L. Drachev ◽  
S.M. Dracheva
Keyword(s):  
Quantitative Analysis ◽  
Cytochrome C ◽  
Absorption Spectra ◽  
Thermodynamic Characteristic ◽  
Reaction Centers ◽  
Differential Absorption ◽  
Rhodopseudomonas Viridis

STUDY OF ABSORPTION SPECTRA OF THE COMPLEXES OF BOVINE SERUM ALBUMIN WITH HOECHST 33258 AND METHYLENE BLUE

2021 ◽  
Vol 55 (2 (255)) ◽  
pp. 158-164
Author(s):  
Nara H. Petrosyan
Keyword(s):  
Methylene Blue ◽  
Serum Albumin ◽  
Absorption Spectra ◽  
Hoechst 33258 ◽  
Differential Absorption ◽  
Partial Loss ◽  
Groove Binding ◽  
Compact Structure ◽  
Binding Material ◽  
Molecular Compounds

The study on the interaction of DNA-specific low-molecular compounds – groove binding material Hoechst 33258 and intercalating ligand methylene blue (MB) with serum albumin has been carried out. The absorption and differential absorption spectra of complexes of the mentioned ligands with protein were obtained. Changes of the absorption and differential absorption spectra indicate the binding of two ligands with albumin. The obtained results indicate that at the interaction with both ligands, the conformational state of the protein alters, though these changes are not similar, since in the case of MB a compactization of the protein folding occurs, while in the case of Hoechst 33258, most apparently, an unfolding of the compact structure takes place as a result of partial loss of helicity of $\alpha$-structures.

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