Structures of bovine, equine and leporine serum albumin.

By A. Bujacz. Acta Crystallographica Section D: Biological Crystallography, 2012

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Interactions between milk proteins and polyphenols: Binding mechanisms, related changes, and the future trends in the dairy industry (2018, background): “It has two Trp residues of which Trp134 is located near to the protein surface whereas Trp213 is surrounded by a hydrophobic environment in a pocket.([71]) Catechin and epicatechin were found to bind at the surface near to Trp134 residue of BSA which was confirmed with the perturbation of the enviro”