Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange.
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ABSTRACT:
SUBMITTER: Smirnovas V
PROVIDER: S-EPMC3379881 | biostudies-literature | 2011 Apr
REPOSITORIES: biostudies-literature
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Structural organization of brain-derived mammalian prions examined by hydrogen-deuterium exchange.
Smirnovas Vytautas V Baron Gerald S GS Offerdahl Danielle K DK Raymond Gregory J GJ Caughey Byron B Surewicz Witold K WK
Nature structural & molecular biology 20110327 4
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. ...[more]
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