Zafrullah, Mohammad ; Khursheed, Zenab ; Yadav, Sushma ; Sahgal, Deepak ; Jameel, Shahid ; Ahmad, Faizan (2004) Acidic pH enhances structure and structural stability of the capsid protein of hepatitis E virus Biochemical and Biophysical Research Communications, 313 (1). pp. 67-73. ISSN 0006-291X
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00062...
Related URL: http://dx.doi.org/10.1016/j.bbrc.2003.11.088
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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Hepatitis E Virus; ORF2 Protein; Secondary Structure; Denaturation; pH-stability |
| ID Code: | 13116 |
| Deposited On: | 11 Nov 2010 06:51 |
| Last Modified: | 17 Feb 2011 06:33 |
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