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Updated: Jun 3, 2026

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
Published on: October 3, 2012
Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange
Vytautas Smirnovas1, Gerald S Baron, Danielle K Offerdahl
1Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio, USA.
Abstract:
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.

