Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Conformational stability of Syrian hamster prion protein PrP(90-231)

Tools
- Tools
+ Tools

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 ISSN 0002-7863.

Research output not available from this repository.

Request-a-Copy directly from author or use local Library Get it For Me service.

Official URL: http://dx.doi.org/10.1021/ja100243h

Request Changes to record.

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, Engineering and Medicine > 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:
DateEvent
7 July 2010Published
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

Data sourced from Thomson Reuters' Web of Knowledge

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us