Title : Inhibitory mechanism of epicatechin gallate on tyrosinase: inhibitory interaction, conformational change and computational simulation.

Pub. Date : 2020 Jun 24

PMID : 32490491






3 Functional Relationships(s)
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1 Molecular docking results showed that hydrophobic and hydrogen bonding forces played a dominant role in the binding of ECG to tyrosinase, affecting the binding affinity of l-dopa to tyrosinase, leading to a decrease in tyrosinase activity. Levodopa tyrosinase Homo sapiens
2 Molecular docking results showed that hydrophobic and hydrogen bonding forces played a dominant role in the binding of ECG to tyrosinase, affecting the binding affinity of l-dopa to tyrosinase, leading to a decrease in tyrosinase activity. Levodopa tyrosinase Homo sapiens
3 Molecular docking results showed that hydrophobic and hydrogen bonding forces played a dominant role in the binding of ECG to tyrosinase, affecting the binding affinity of l-dopa to tyrosinase, leading to a decrease in tyrosinase activity. Levodopa tyrosinase Homo sapiens