Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 18, Issue 4, Pages 504-506Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2035
Keywords
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Funding
- US National Institutes of Health [NS44158, NS38604, AG14359]
- National Institute of Allergy and Infectious Diseases
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One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrPSc. Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrPSc. Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue similar to 80-90 to the C-terminus, which in PrPSc consists of beta-strands and relatively short turns and/or loops, with no native alpha-helices present.
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