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

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

Author information

1
Department 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.

PMID:
21441913
PMCID:
PMC3379881
DOI:
10.1038/nsmb.2035
[Indexed for MEDLINE]
Free PMC Article

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