Prion Disease Essay

Prion disease is a group of neurodegenerative disorder that affects both humans and animals. It is a type of protein in the brain, when triggered, causes the protein to misfold. Fred E. Cohen at the University of California investigates the connection between protein folding and neurodegenerative disease. Cohen uses thermodynamic and kinetic properties to gain an understanding of infectious, sporadic and inherited form of these diseases. Many proteins are the most prominent structural motif of the functional protein in its native conformation known as the alpha helix (Pauling et al. 1951). When a protein follows the wrong folding pathway, the protein misfolds and becomes a toxic configuration. When a protein becomes toxic, it obtains a motif known as the beta sheet. Although the beta sheet conformation also exists in many functional native proteins, the abnormal conformational change from alpha helix to beta sheet exposes

They are a misfolded form of normal cell proteins with a distinctive ability to convert their normal folded complements into more prions, The ability to fold as a helix or a sheet depends on its constituent amino acid. Altering a single amino acid changes the folded form of a protein. Cohen’ s study utilizes one of the known prion proteins, the PrP gene, as a model to examine how naturally occurring amino acid mutations could disrupt normal protein structure to induce it to misfold. Prions, the causative agent of most prion diseases are composed of primarily of abnormal prion (PrPSc) which replicates through the recruitment and conformational conversion of the host encoding cellular prion (PrPC). Energetic analyses were used to determine what therapeutic interventions that decreased production, state stability and the kinetic barrier to misfolding or