Assignment of disulfide bonds in the X protein (HBx) of hepatitis B virus

Aparna Gupta, Tapas Mal, N. Jayasuryan, Virander S. Chauhan

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

We have established the disulphide arrangement of cysteines in E. coli expressed HBx by chromatographic analysis of enzymatically cleaved protein and sequence analysis of cysteine containing fragments. Eight of the nine cysteines are disulphide linked in an interesting pattern. Each cysteine is linked to the fourth cysteine in a sequential manner and the last cysteine is free; the disulphide linkages are between Cys7 and Cys78, CyS17 and Cys115, Cys61 and Cys137, Cys69 and Cys143 while Cys148 is free.

Original languageEnglish (US)
Pages (from-to)919-924
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume212
Issue number3
DOIs
Publication statusPublished - Jul 26 1995

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this