Abstract
The peculiarities of the complexation of bovine serum albumin (BSA) and quercetin (Q) are shown in the article. The static mechanism of the formation of BSA-Q conjugates with the predominant effect of hydrogen bonds and hydrophobic interaction is established from fluorescence and absorption spectral data of aqueous solutions at different temperatures. The detailed analysis of an interaction of the molecules is performed in a molecular modeling procedure, including docking and molecular dynamics study. The computation results match the experimental outcome.
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