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This technology is a novel chemistry approach for single-site-specific cysteine modification under physiologically relevant conditions. This technology is able to site specifically modify the cysteine in a four residue peptide sequence, X-Cys-Pro-X, where X is an aromatic amino acid (Phe, Trp, or Tyr), while other cysteines or reactive functional groups on the same peptide protein chain remain intact. In the specific sequence, the amino acid proline induces the formation of a β-turn that allows the two aromatic amino acid residues to form a local Pi-clamp around the cysteine thiol.