Abstract

The sulfation of tyrosine residues is one of the most popular post-translational modifications for peptides and proteins [1]. It has been proposed that the sulfate plays an important role in the specific protein–protein interactions during protein transport. The negative charge of a tyrosineO-sulfate [Tyr(SO3 H)] residue should participate in these interactions, but little is known about their detailed chemical principles. In this study, we investigated the interaction of a Tyr(SO3 H) residue with cationic functional groups on the same peptide chain and on externally added basic peptides.

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