Conformational changes and surface binding property of rat liver Cd5Zn2-metallothionein

A series of conformational changes of native rat liver metallothionein were observed under different ionic strength by 1H NMR. Furthermore, binding of magnetic probes to MT gives us an implication that positively charged groups of lysine are not completely folded back towards the inner core of metallothionein, the negatively charged metal-sulfur core is slightly exposed to the solvent.