Understanding the Biochemistry of BSE - Essay Example

Amino acids involved include Alanine, Valine and Leucine (Branden & Tooze, 1999). Hydrogen Bonds: Hydrogen bonds are formed when a hydrogen is shared by two partially charged atoms of an amino acid side chain. An example is interaction between the Aspartate and Serine; Oxygen in Asp carries a partial negative charge and Hydrogen in Serine carries a partial positive charge. The two interact forming a hydrogen bond (Branden & Tooze, 1999). Ionic Bonds: Ionic bonds are formed among polar side chains of amino acids.

Opposite (Negative and Positive) charges interact to form an ionic bond. An example is interaction between positively charged Arginine and negatively charged Glutamate to form an ionic bond (Branden & Tooze, 1999). Chaperone proteins bind to newly synthesized protein and ensure that the newly synthesized protein is properly folded into its anticipated structure. In Bovine Spongiform Encephalopathy, the prion PrPSc (Prion protein Scrapie Associated) acts as the chaperone for normal cellular protein PrPC (MeganSimmer, 2006).

As a chaperone, PrPSc binds to newly synthesized cellular protein PrPC and induces folding. The α-helical PrPC is misfolded into an abnormal β-pleated sheet conformation PrPSc. This new conformation is lethal and the known cause of neurodegenerative Bovine Spongiform Encephalopathy or Mad Cow Disease (Hargrove, 2010). Compared to other chaperones, PrPSc induces conformational changes that yields a protein with a structure identical to itself. The resultant protein is disease causing in nature.

Other chaperones, example Hsp60 and Hsp70 give off functional proteins of independent secondary and tertiary structure after proper folding (Branden & Tooze, 1999) (Hargrove, 2010). Bovine Spongiform Encephalopathy or Mad cow disease is caused by misfolding of normal cellular prion PrPC. This misfold is induced by the disease causing prion PrPSc. Prions (abbreviation for ‘Proteinaceous