We propose to use SAXS to study the self-association of the prion proteins. Structural transformation of these proteins is believed to be at the basis of a range of transmissible neurodegenerative prion diseases, of which examples include Creutzfeld Jacob Disease (CJD) in humans, Scrapie in sheep and Bovine Spongiform Encephalopathy (BSE) - or """"""""mad cow disease"""""""". Heat-induced isomerization of the alpha-helical conformation of a recombinant form of the prion protein, alpha-rPrP to a multimeric beta-sheet form will be studied using SAXS. By measuring a series of scattering profiles during the time course of the isomerization reaction, it will be possible to determine the polydispersity of the resulting multimeric form and see how this depends on solvent conditions and also on various mutations which can be generated in the recombinant rPrP.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-20
Application #
6322179
Study Section
Project Start
1999-03-01
Project End
2000-04-14
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
20
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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