Abstract
Hepatitis E virus (HEV) is enterically transmitted and endemic to tropical areas of the world. The major capsid protein of HEV is pORF2 (∼74 kDa), encoded by open reading frame 2 (ORF2). When expressed in insect cells, it is processed into a ∼55 kDa form (n-pORF2). We also generated a mutant, m-pORF2, lacking a C-terminal hydrophobic region shown earlier to be required for its homo-oligomerization. Circular dichroism was used to measure the secondary structure and stability of these proteins as a function of pH and temperature. With decreasing pH both proteins acquired increasing α-helicity and thermal stability in terms of midpoint of denaturation and the Gibbs energy change.
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