Biochem Task Essay
Task 2: Protein Structure
E. Explain the four forces (i.e., bonds or interactions) that stabilize a protein’s structure at the tertiary level.
Hydrophobic interactions- R group in the amino acid is non-polar and therefore will avoid contact with water by joining together in the interior of the molecule, it will avoid contact with water.
Van der Waals- this interaction occurs when the hydrophobic R groups that are packed together have a weak attraction that helps to reinforce the hydrophobic bond.
Ionic bonding- The R group must have a charge. In this case the opposites attract (positive to …show more content…
2. Explain one possible role of a chaperone protein in BSE, including each of the following:
● how chaperones normally act in the cell
Chaperone proteins normally help a cell fold properly. In BSE, the disease hijacks the chaperone proteins and uses them to help misfold the protein and help the disease protein propagate. (Jones)
● how a chaperone protein can contribute to BSE
When the chaperone protein is “hijacked”, the disease causing prion is using the mechanics of the chaperone to ensure that all future proteins will be misfolded and be a diseased protein. In this way the disease causing prion becomes self propagating. (Jones)
3. Recommend two ways that a country without regulations in place can decrease the risk of transmitting the prion involved in BSE (e.g., feeding practices, animal disposal).
Two ways to decrease the risk of the BSE prion is by excluding animals that are greater than thirty months old from food supplies and by having a ban all all feed that has animal or animal byproducts in them from the feed supply to live animals. ("Control Measures")
Amino Acids. (n.d.). Retrieved November 29, 2015, from