Essay on Biochem Task 2

877 Words Aug 25th, 2015 4 Pages
1.A. Original model of an essential amino acid Phenylalanine. This shows the atoms and bonds in both the backbone and the side chain.

B. Original diagram of the different levels of protein structure (i.e., primary, secondary, tertiary, and quaternary).

C. An original diagram, that demonstrates how a peptide bond is made through dehydration, using a complete chemical equation.

Citation: Hudon-MIller, S. (2013).

D. An original diagram, that demonstrates how a peptide bond is broken through hydrolysis, using a complete chemical equation.

Citation: Hudon-MIller, S. (2013).
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They result in a change in the structure resulting in hydrophobic proteins, these new prions congregate with other PrPsc proteins resulting in plaque or “aggregation” on the neuron.
Prions (PrPsc) influence the PrPc proteins they come in contact with to misfold and begin to aggregate. The aggregation leads to development of fibers or plaques. The aggregation of PrPsc around the neurons triggers the cell to self destruct. It is also able to spread to nearby neurons resulting in areas of neuronal death which results in the brain tissue having spaces of void which appear like a sponge. J. Thompson (2014)

2. In a healthy cell floating in the cytoplasm are proteins we refer to as “chaperones” because they instruct or guide the folding of younger proteins. They guide them through the folding process resulting in perfectly structured protein. That performs its function as it should. When chaperones go bad aka Prions, as is the case in Bovine Spongiform Encephalopathy (BSE), we see the wide spread destruction that can occur when mutations in the folding occur. In Bovine Spongiform Encephalopathy the PrPsc protein acts as a chaperone and influences the PrPc protein it comes in contact with, to misfold which results in a new structure this new form iis hydrophobic (PrPsc). As these proteins form they aggregate with other PrPsc proteins. As the PrPsc proteins aggregate they trigger the neuron to self destruct which

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