https://www.selleckchem.com/products/pd173212.html
The binding interactions of bioactive compounds with proteins are of great importance in the food, biochemistry and pharmaceutical fields. Herein, the binding mechanisms between 5-O-caffeoylquinic acid (5-CQA) and ovalbumin (OVA) were investigated by multi-spectroscopic studies combined with docking and molecular dynamics (MD) simulations. The emission intensity of OVA was quenched by 5-CQA and Stern-Volmer analysis indicated the existence of a static suppression by OVA-5-CQA complex formation. Thermodynamic parameters revealed that th
Like
Comment
Share
