Abstract

pKa-Values of lysine residues of mammalian metallothionein were determined by chemical titration measurements of ɛ-CH2 lysine resonances in the1H-NMR spectra. They are about 0.5 pH-unit higher than the average pKa-value of a metal-free derivative, suggesting interaction of the positively charged residues with the two three-fold negatively charged metal-thiolate clusters of the metal-containing form. Deprotonation of the lysines leads to circular dichroism changes attributable to an electrostatically induced structural transition of the protein.

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