Prion Protein Structure and Human Disease

Abstract

Prions, misfolded proteins that act as pathogenic and infectious agents, are a topic of great biochemical and medical importance. They are the underlying cause of several neurodegenerative diseases including Creutzfeldt-Jakob disease (CJD), Gerstmann-Staussler-Scheinker syndrome (GSS), and fatal familial insomnia, which although rare are rapid in their progression and unquestionably fatal. The misbehavior of the culprit protein, relates to one of the most essential concepts in the study of biomolecules; mainly, that the sequence of a protein determines its shape which in turn dictates its function. A key area of research for studying the effects and causes of familial prion disease includes in depth examination of the protein structure in both the normal and diseased states. Recent investigations in this area have made use of a wide range of technological methods including molecular dynamic simulations and nuclear magnetic resonance imaging. These articles have contributed to a deeper understanding of prions and will hopefully lend to further investigations that may determine methods of treating these deadly diseases.