| Summary: | 碩士 === 國立交通大學 === 生物科技學系 === 100 === Metallothionein-green fluorescence fusion protein (MT-GFP) is a zinc binding protein, which binds seven divalent transition metal ions through its 20 conserved cysteines and forms two metal binding clusters with Zinc-Blende structure. In this study, Mn2+ ions has substituted for Zn2+ at M3, M4 metal binding sites in the β-domain of MT-GFP. We found this Mn, Zn binding protein exhibits weak ferromagnetic properties at temperature range from 10K to 300K by SQUID measurement. By micro-Raman spectroscopy analysis, the Zn-S and Mn-S bending modes can be observed clearly at 288 cm-1 and 355 cm-1, respectively. These evidences indicate that the Zn2+ and Mn2+ ions are bound with Cys residues of MT-GFP. Extended X-ray absorption fine structure (EXAFS) analysis also indicats Mn2+ ions bond to MT-GFP via the Mn-S bond of Cys. The conformation of Mn,Zn-MT-GFP can be characterized by TEM and the its intermolecular interactions can be determined by its electron diffraction pattern.
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