Structural organization of brain-derived mammalian prions as probed by hydrogen exchange

@inproceedings{Smirnovas2011StructuralOO,
  title={Structural organization of brain-derived mammalian prions as probed by hydrogen exchange},
  author={Vytautas Smirnovas and Gerald S. Baron and Danielle K Offerdahl and Gregory J. Raymond and Byron Caughey and Witold K Surewicz},
  booktitle={Nature Structural &Molecular Biology},
  year={2011}
}
One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrPSc. Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80–90 to the C-terminus, which in PrPSc consists of β-strands and relatively short turns and/or loops, with no native α-helices present. 
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