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. 2016 Apr 5;11(4):e0153002. doi: 10.1371/journal.pone.0153002

Fig 6. Changes in the electrostatic interaction of lysine residues as a consequence of oxidative deamination.

Fig 6

(A) Schematic representation of the EGCG binding site in subdomains IIA and IIIA. Electrostatic interactions between Lys-432 and Asp-187 and between Lys-444 and Glu-292 are shown with yellow arrows. (B) Time dependent evolution of distance between the Lys-432 ε-carbon and the carboxyl group (γ-COOH) of Asp-187 before and after AAS formation at Lys-432. (C) Time dependent evolution of distance between the Lys-444 ε-carbon to the carboxyl group (δ-COOH) of Glu-292 before and after AAS formation at Lys-444.