FIBER DIFFRACTION FROM AMYLOID FILAMENTS

这个子项目是众多研究子项目之一

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for 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.