A Novel Structurally Stable Multiepitope Protein for Detection of HCV

Figure 5

Structural analysis of rMEHCV by circular dichroism. (a) Far-UV CD spectra of rMEHCV (2.5 μM) at 25°C in 5 mM Tris-HCl pH 7.0 (gray line) and pH 8.0 (black line). The table inset shows the secondary structure content of protein in both pHs; (b) Far-UV CD spectra of rMEHCV (2.5 μM) in 5 mM Tris-HCl (pH 7.0) as a function of temperature. The arrow indicates the increase of temperature from 25 to 85°C, in which the complete loss of CD signal was observed; (c) Far-UV CD spectra of rMEHCV (2.5 μM) in 5 mM Tris-HCl (pH 8.0). The arrow indicates the increase of temperature from 25 to 95°C, in which the CD signal reducing until ~3,500 deg·cm²·dmol⁻¹ was observed.

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