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In fact, the Cu 2+ -histidine interaction (binding) in nature can match the importance of iron (Fe 2+ ) binding with proteins, and the consequent haem interactions that support the very existence of life ( Intriguingly, the interactions of N-terminal histidine residues of the prion protein (PrP) mainly with Cu 2+ sequestration and accumulation in diseased brain (T 2+ at neutral pH (7.4) ( 2+ is not necessarily pathogenic since it has also been found to produce neuroprotection due to the cis interaction with the C terminal of PrP

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The N-terminal methionine oxidizes, creating methionine sulfoxide that alters binding kinetics