Acidic pH enhances structure and structural stability of the capsid protein of hepatitis E virus |
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Authors: | Zafrullah Mohammad Khursheed Zenab Yadav Sushma Sahgal Deepak Jameel Shahid Ahmad Faizan |
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Institution: | Department of Biosciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India. |
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Abstract: | Hepatitis E virus (HEV) is enterically transmitted and endemic to tropical areas of the world. The major capsid protein of HEV is pORF2 ( approximately 74 kDa), encoded by open reading frame 2 (ORF2). When expressed in insect cells, it is processed into a approximately 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 alpha-helicity and thermal stability in terms of midpoint of denaturation and the Gibbs energy change. |
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Keywords: | Hepatitis E virus ORF2 protein Secondary structure Denaturation pH-stability |
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