Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange

Nat Struct Mol Biol. 2011 Apr;18(4):504-6. doi: 10.1038/nsmb.2035. Epub 2011 Mar 27.


One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrP(Sc). Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrP(Sc). 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 PrP(Sc) consists of β-strands and relatively short turns and/or loops, with no native α-helices present.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Animals
  • Brain Chemistry*
  • Deuterium
  • Hydrogen
  • Mass Spectrometry
  • Prions / chemistry*


  • Prions
  • Hydrogen
  • Deuterium