The aim of the research in our lab is to understand the conformational transitions of proteins associated with amyloid diseases. Alzheimer and prion diseases belong to amyloid diseases for which a normal host polypeptide accumulates in an abnormal beta-sheet-rich form in fibrillar aggregates. In prion diseases, the mostly alpha-helical host prion protein undergoes a conformational switch to a structure with enhanced beta-sheet content. It is believed that this converted abnormal form of the prion protein is the infectious agent of bovine spongiform encephalopathy (BSE), scrapie in sheep, and Creutzfeldt-Jakob disease (CJD) in humans. In Alzheimer's disease, a peptide with mostly a random coil-like structure is converted to a beta-sheet-rich polypeptide clustered in fibrils. Since, in both mentioned systems a structural transition is associated with disease, a detailed knowledge of the structures and dynamics of the normal and the abnormal conformers are of highest interest. We have determined the structures of the normal forms of the prion protein and of the Alzheimer's peptide. Further studies will include the structural elucidation of the abnormal conformations of these diseases. We use a variety of techniques to solve the structures and to study the conformational transition of amyloidogenic proteins including as a major experimental tool Nuclear Magnetic Resonance Spectroscopy (NMR).