Grabenauer, Megan, Wyttenbach, Thomas, Sanghera, Narinder, Slade, Susan E., Pinheiro, Teresa J. T., Scrivens, James H. and Bowers, Michael T. (2010) Conformational stability of Syrian hamster prion protein PrP(90-231). Journal of the American Chemical Society, Vol.132 (No.26). pp. 8816-8818. doi:10.1021/ja100243h

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Abstract

Many transmissible spongiform encephalopathies (TSEs) are believed to be caused by a misfolded form of the normal cellular prion protein (PrPC) known as PrPSc. While PrPSc is known to be exceptionally stable and resistant to protease degradation, PrPC has not shown these same unusual characteristics. However, using ion mobility spectrometry mass spectrometry (IMS-MS), we found evidence for at least one very stable conformation of a truncated form of recombinant PrPC consisting of residues 90-231, which resists unfolding in the absence of solvent at high injection energies and at temperatures in excess of 600 K. We also report the first absolute collision cross sections measured for recombinant Syrian hamster prion protein PrP(90-231).

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Divisions:	Faculty of Science > Life Sciences (2010- ) > Biological Sciences ( -2010)
Journal or Publication Title:	Journal of the American Chemical Society
Publisher:	American Chemical Society
ISSN:	0002-7863
Official Date:	7 July 2010
Dates:	Date Event 7 July 2010 Published
Volume:	Vol.132
Number:	No.26
Number of Pages:	4
Page Range:	pp. 8816-8818
DOI:	10.1021/ja100243h
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Department for Environment, Food and Rural Affairs, U.K., National Institutes of Health
Grant number:	IPOIAG027818-010003

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