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

Yaghoobi, Hajar. and Bandehpour, Mojgan. (2017) Effect of Human HSP90 on Secondary and Tertiary Structures of Core Protein of Hepatitis C Virus and HbsAg of Hepatitis B Virus. Trends in Peptide and Protein Sciences, 1 (2).

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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.

Item Type: Article
Uncontrolled Keywords: Core protein,HbsAg,Circular dichroism
Subjects: WI Digestive System
Divisions: Faculty of Medicine
Depositing User: Users 1 not found.
Date Deposited: 04 Nov 2017 09:25
Last Modified: 23 Apr 2018 10:17
URI: http://eprints.skums.ac.ir/id/eprint/6229

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