Abstract
The secondary structure of recombinant proteins can change through complex formation with other proteins. Here, we have determined the spatial structure of two proteins, including core protein of hepatitis C virus and HbsAg of hepatitis B virus, without the effect of human HSP90 as well as with the effect of this recombinant chaperone. As a result, the increase in intensity from 297.5 to 346.64 was accompanied by different folding and being non-polar protein in complex with the chaperone. HbsAg protein, combined with HSP90, showed a reduction in the maximum peak wavelength from 385 to 369.07 nm. The property of protein of being non-polar and hydrophobic, as well as having an increase in intensity from 200 to 219, indicates the protein folding. The shift from 342 to 337 nm along with blue shift indicates hydrophobic properties and the removal of protein from the water environment. Highlights: The structure of recombinant protein is very important in vaccine complex with an adjuvant. The immunity of HCV core and HbsAg proteins could increase in complex with HSP90. Fluorescence spectroscopy and circular dichroism were used to determine the proteins structure. Structural data confirmed the hydrophobic properties if proteins changed in complexation with HSP90.
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