Fourier transform IR and Fourier transform Raman spectroscopy studies of metallothionein-III: amide I band assignments and secondary structural comparison with metallothioneins-I and -II |
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Authors: | Shi Yan-Bo Fang Jiang-Lin Liu Xiao-Yu Du Liang Tang Wen-Xia |
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Institution: | State Key Laboratory of Coordination Chemistry, Coordination Chemistry Institute, Nanjing University, Nanjing 210093, China. |
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Abstract: | The secondary structures of porcine brain Cu(4)Zn(3)-metallothionein (MT)-III and Cd(5)Zn(2)MT-I, Cd(5)Zn(2)MT-II, and Zn(7)MT-I from rabbit livers in the solid state are investigated by Fourier transform IR spectroscopy (FTIR) and Fourier transform Raman spectroscopy (FT-Raman). The Cu(4)Zn(3)MT-III contains 26-28% beta-turns and half-turns, 13-14% 3(10)-helices, 47-49% random coils, and 11-12% beta-extended chains. The structural comparison of porcine brain Cu(4)Zn(3)MT-III with rabbit liver Cd(5)Zn(2)MT-I (II) and Zn(7)MT-I shows that the contents of the random coil structure are obviously increased. The results indicate that the insert of an acidic hexapeptide in the alpha domain of Cu(4)Zn(3)MT-III possibly forms an alpha helix. However, because the bands assigned to the alpha-helix and random coil structures are overlapped in the spectra, the content of random coil structures in Cu(4)Zn(3)MT-III is therefore higher than those in Cd(5)Zn(2)MT-I, Cd(5)Zn(2)MT-II, and Zn(7)MT-I. |
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Keywords: | Fourier transform IR spectroscopy Fourier transform Raman spectroscopy metallothionein‐III (growth inhibitory factor) secondary structure amide I band |
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