title: Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange.
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.
authors: Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio, USA.
authors: Vytautas
authors: V
authors: Smirnovas
authors: Gerald S
authors: GS
authors: Baron
authors: Danielle K
authors: DK
authors: Offerdahl
authors: Gregory J
authors: GJ
authors: Raymond
authors: Byron
authors: B
authors: Caughey
authors: Witold K
authors: WK
authors: Surewicz
mesh_terms: D000818:Animals; D001923:Brain Chemistry; D003903:Deuterium; D006859:Hydrogen; D013058:Mass Spectrometry; D011328:Prions / Q000737:chemistry*
chemical_list: D011328:Prions; D006859:Hydrogen; D003903:Deuterium