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. 2007 Nov 22;36(3):712–725. doi: 10.1093/nar/gkm1051

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© 2007 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Far-UV CD analysis of core proteins. Far-UV CD spectra of HCV (A), GBV-B (B), WNV (C) and BVDV (D) core proteins. Measurements were done in 20 mM sodium phosphate buffer (pH 7.4) containing 5 mM 2-mercaptoethanol. For HCV and GBV-B core proteins, the buffer also contained 0.1% n-dodecyl β-d-maltoside (DM). Spectra were recorded at 20°C, at 95°C after slow heating of the protein, and again at 20°C after slow cooling. Melting curves were recorded at 222 nm, during the heating and cooling processes. Secondary structure content was calculated by the k2d method of spectral deconvolution (http://www.cryst.bbk.ac.uk/cdweb/html/home.html).

Figure 6. — Far-UV CD analysis of core proteins. Far-UV CD spectra of HCV (A), GBV-B (B), WNV (C) and BVDV (D) core proteins. Measurements were done in 20 mM sodium phosphate buffer (pH 7.4) containing 5 mM 2-mercaptoethanol. For HCV and GBV-B core proteins, the buffer also contained 0.1% n-dodecyl β-d-maltoside (DM). Spectra were recorded at 20°C, at 95°C after slow heating of the protein, and again at 20°C after slow cooling. Melting curves were recorded at 222 nm, during the heating and cooling processes. Secondary structure content was calculated by the k2d method of spectral deconvolution (http://www.cryst.bbk.ac.uk/cdweb/html/home.html).