Effect of Human HSP90 on Secondary and Tertiary Structures of CoreudProtein of Hepatitis C Virus and HbsAg of Hepatitis B Virus

摘要

The secondary structure of recombinant proteins can change through complex formationudwith other proteins. Here, we have determined the spatial structure of two proteins,udincluding core protein of hepatitis C virus and HbsAg of hepatitis B virus, without theudeffect of human HSP90 as well as with the effect of this recombinant chaperone. As audresult, the increase in intensity from 297.5 to 346.64 was accompanied by different foldingudand being non-polar protein in complex with the chaperone. HbsAg protein, combinedudwith HSP90, showed a reduction in the maximum peak wavelength from 385 to 369.07udnm. The property of protein of being non-polar and hydrophobic, as well as having anudincrease in intensity from 200 to 219, indicates the protein folding. The shift from 342 toud337 nm along with blue shift indicates hydrophobic properties and the removal of proteinudfrom the water environment.