Hepatitis B virus capsid particles are assembled from core-protein dimer precursors.

@article{Zhou1992HepatitisBV,
  title={Hepatitis B virus capsid particles are assembled from core-protein dimer precursors.},
  author={Shubo Zhou and David N. Standring},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1992},
  volume={89 21},
  pages={10046-50}
}
Our studies on the assembly of hepatitis B virus capsids or core particles in Xenopus oocytes have demonstrated that unassembled p21.5 core proteins ("free p21.5") provide a pool of low-molecular-mass precursors for core-particle assembly. Here we have characterized this material. Free p21.5 sedimented through gradients of 3-25% sucrose (wt/vol) as a single protein species of approximately 40 kDa, corresponding to a p21.5 dimer. On nonreducing SDS/polyacrylamide gels, free p21.5 migrated as… CONTINUE READING

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