Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution.

@article{Kozin2001SheepPP,
  title={Sheep prion protein synthetic peptide spanning helix 1 and beta-strand 2 (residues 142-166) shows beta-hairpin structure in solution.},
  author={Sergey A Kozin and Gildas Bertho and Alexey K. Mazur and Hanitra Rabesona and Jean Pierre Girault and Thomas Haertl{\'e} and Mitsuo Takahashi and Pascale Debey and G. Hui Bon Hoa},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 49},
  pages={46364-70}
}
According to the "protein only" hypothesis, a conformational conversion of the non-pathogenic "cellular" prion isoform into a pathogenic "scrapie" isoform is the fundamental event in the onset of prion diseases. During this pathogenic conversion, helix H1 and two adjacent surface loops L2 and L3 of the normal prion protein are thought to undergo a conformational transition into an extended beta-like structure, which is prompted by interactions with the pre-existing beta-sheet. To get more… CONTINUE READING

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