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. 2017 Mar 3;7:43160. doi: 10.1038/srep43160

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Copyright © 2017, The Author(s)

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(A) Western blotting (cropped blot) and (B) Circular Dichroism (CD) analysis of WT-HBc particles. Denatured HBc samples were subjected to SDS-PAGE followed by immuno-blotting using anti-6-His and anti-HBc antibodies. Results confirmed the presence of specific protein bands at 21 kDa. CD graph shows the overall conformation of far-UV CD analysis of WT-HBc core particles. WT-HBc (C) (solid line) and WT-HBc (I) (dashed line) exhibited spectra typical of α-helix-containing proteins with minima at 220 and 208 nm. The CD spectra are typical of WT-HBc core monomer secondary structure.