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The pantheon of characterized copper chaperone proteins includes notable entities, such as antioxidant protein 1 (ATOX1), copper chaperone for superoxide dismutase (CCS) and cytochrome c oxidase copper chaperone (COX17)

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For example, at a very conservative guestimate (taking the lowest of the range of hydrogen bond energies above 12 kJ/mole and just a thousand water molecules associated with a proteins hydrophilic domains), one arrives at a figure of around 12,000 kJ/mole for their collective energy (assuming each water molecule forms just one hydrogen bond with a neighbour or the protein: a water molecule can form up to four hydrogen bonds with its neighbours [Jorgensen and Madura, 1985])

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