Conformational change in hamster scrapie prion protein (PrP27-30) associated with proteinase K resistance and prion infectivity.

@article{Suzuki2008ConformationalCI,
  title={Conformational change in hamster scrapie prion protein (PrP27-30) associated with proteinase K resistance and prion infectivity.},
  author={Sachiko Y Suzuki and Masuhiro Takata and Kenta Teruya and Morikazu Shinagawa and Shirou Mohri and Takashi Yokoyama},
  journal={The Journal of veterinary medical science},
  year={2008},
  volume={70 2},
  pages={159-65}
}
The scrapie prion protein (PrP27-30) is a crucial component of the prion and is responsible for its transmissibility. Structural information on this protein is limited because it is insoluble and shows aggregated properties. In this study, PrP27-30 was effectively dispersed using sonication under the weak alkaline condition. Subsequently, the small PrP27-30 aggregates were subjected to different pH, heat, and denaturing conditions. The loss of proteinase K (PK) resistance of PrP27-30 and prion… CONTINUE READING

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