- describe experimental evidence to show that protein misfolding and aggregation depends on the amino acid sequence and the environment in which folding occurs.
- describe conditions in vitro that may promote aggregation and how these might be minimized in vivo
- describe alternative conformations of prion proteins and relate them to a energy topology landscape
- explain how prion diseases may be transmitted in the absence of genetic material
Thumbnail: Structure of human hemoglobin. The proteins α and β subunits are in red and blue, and the iron-containing heme groups in green. From PDB: 1GZX. (GNU; Proteopedia Hemoglobin).