Conformational properties of beta-PrP.

  title={Conformational properties of beta-PrP.},
  author={Laszlo L. P. Hosszu and Clare R. Trevitt and Samantha L. Jones and Mark Batchelor and David J. Scott and Graham S. Jackson and John Collinge and J. P. Waltho and A. R. Clarke},
  journal={The Journal of biological chemistry},
  volume={284 33},
Prion propagation involves a conformational transition of the cellular form of prion protein (PrPC) to a disease-specific isomer (PrPSc), shifting from a predominantly alpha-helical conformation to one dominated by beta-sheet structure. This conformational transition is of critical importance in understanding the molecular basis for prion disease. Here, we elucidate the conformational properties of a disulfide-reduced fragment of human PrP spanning residues 91-231 under acidic conditions, using… CONTINUE READING
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