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 language | English (US) |
|---|---|
| Pages (from-to) | 919-924 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 212 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jul 26 1995 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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