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- W2926013595 abstract "Flavonoids exhibit a wide variety of biological effects and hold great protein-binding potential. In this study, we take quercetin, an extensively studied flavonoid, as an example to investigate the structural basis underlying their excellent protein-binding ability. Through calculating the pocket similarity of quercetin-binding proteins and comparing the binding modes between quercetins bound with different proteins, it was found that the great protein-binding capacity of quercetin not only arises from the structural conservation of target proteins, but also stems from its unique structure, in which molecular rigidity and flexibility is well-balanced and various chemical interactions could be formed between the small molecule and protein targets." @default.
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- W2926013595 date "2017-11-01" @default.
- W2926013595 modified "2023-09-28" @default.
- W2926013595 title "Structural Basis for Great Protein-Binding Potential of Flavonoids: A Case Study of Quercetin" @default.
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- W2926013595 doi "https://doi.org/10.1177/1934578x1701201142" @default.
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