This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Amyloids are formed when proteins change conformation to form insoluble fibers that can cause severe damage and death. Amyloidoses include Alzheimers disease and a variety of prion diseases including Creutzfeldt-Jakob and BSE (mad cow disease). Mammalian prions are formed by the protein PrP. Amyloid proteins share a cross-beta structure, but have resisted characterization by crystallography and NMR. Fiber diffraction, in combination with electron microscopy, offers the best hope for structure determination. Structural studies are needed to answer fundamental protein folding questions, to understand amyloid formation, and for rational drug design.We use oriented sols and dried fibers made in high magnetic fields under controlled conditions. Improved prion availability, improved methods of specimen preparation, and synchrotron radiation offer unprecedented opportunities to obtain improved amyloid diffraction data.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR008630-12
Application #
7601776
Study Section
Special Emphasis Panel (ZRG1-BCMB-E (40))
Project Start
2007-04-01
Project End
2008-03-31
Budget Start
2007-04-01
Budget End
2008-03-31
Support Year
12
Fiscal Year
2007
Total Cost
$20,641
Indirect Cost
Name
Illinois Institute of Technology
Department
Other Basic Sciences
Type
Schools of Arts and Sciences
DUNS #
042084434
City
Chicago
State
IL
Country
United States
Zip Code
60616
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