CD and NMR Studies of Prion Protein (PrP) Helix 1

@article{Ziegler2003CDAN,
  title={CD and NMR Studies of Prion Protein (PrP) Helix 1},
  author={Jan Ziegler and Heinrich Sticht and Ute C. Marx and Wolfgang M{\"u}ller and Paul Rösch and Stephan Schwarzinger},
  journal={Journal of Biological Chemistry},
  year={2003},
  volume={278},
  pages={50175 - 50181}
}
The conversion of prion helix 1 from an α-helical into an extended conformation is generally assumed to be an essential step in the conversion of the cellular isoform PrPC of the prion protein to the pathogenic isoform PrPSc. Peptides encompassing helix 1 and flanking sequences were analyzed by nuclear magnetic resonance and circular dichroism. Our results indicate a remarkably high instrinsic helix propensity of the helix 1 region. In particular, these peptides retain significant helicity… 

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