Mad Cow Disease

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GRT TASK 2 BSE Diagram of Essential Amino Acid Lysine ● ● ● ● ● ● ● Lysine is a base Physical properties: Polar, positively charged Highly reactive Hydrophilic Solubility: ^ soluble in cold water Reactivity: 0 Flammability: 1 (may be combustible at high temps Protein Structure Dehydration Hydrolysis Stabilizing Forces 1) Hydrophobic Interactions Non polar amino acids (leucine and phenylalanine are two examples). Weakest type of bond. Hydrogen bonds: Polar or charged amino acids (example Tyrosine). Weak interaction but stronger than the hydrophobic interaction Ionic Bonds: Charged amino acids (Lysine and Aspartic acid are examples). Opposite attract. Little stronger than hydrogen bond but weaker than the bond between polypeptides Disulfide bond: Only occurs between 2 cysteine amino acids. Forms sulfur sulfur link (disulfide like). Strong interaction. 2) 3) 4) Bovine Spongiform Encephalopathy protein misfolding ● ● ● ● ● ● ● ● ● ● Better known as Mad Cow Disease Cause by an abnormal form of prions which are proteins Slowly progressive disease that affects a cow’s central nervous system Cattle are infected by eating food that have remains of other animals like cattle and sheep that contain the infectious prions There are normal proteins (PrPc) and abnormal harmful prions (PrPsc). The prion is a misfolded form of PrPc. Cells have chaperones for young proteins to help it fold correctly Prions affect the folding of normal, healthy proteins PrPc comes in contact with PrPsc, PrPsc affects the folding of the normal protein and causes it to fold into the harmful form of the protein PrPsc is hydrophobic. It congregates with other PrPsc proteins forming plaques Plaques cause neuronal cell death leaving holes that resemble a sponge. Role of Prions in BSE ● ● ● ● A prion is an infectious, abnormally folded protein PrPsc is the abnormal

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