Question details:

Competency 208.5.2: Amino Acids and Peptide Bonds, Protein Structure – The graduate can construct models of the structure and function of amino acids and peptide bonds, predict ionization of an amino acid, and demonstrate peptide bond breaking; demonstrate how protein structure affects susceptibility or resistance to disease.

Objectives

208.5.2-01:Constructa model of an essential amino acid with side chains.

208.5.2-02: Identify a given amino acid by its chemical characteristics.

208.5.2-04: Demonstrate how a peptide bond is made or broken through dehydration or hydrolysis respectively.

208.5.2-05: Distinguish between primary, secondary, tertiary, and quaternary protein structure.

208.5.2-06: Explain the forces that stabilize a protein’s three-dimensional native structure.

208.5.2-07: Demonstrate how proteins at a molecular level are responsible for susceptibility or resistance to a pathogen such as mad cow disease.

Introduction:

Bovine spongiform encephalopathy (BSE), also known as mad cow disease, is a worldwide problem. While many countries in the European Union and the United States have regulatory legislation in place to combat the spread of BSE, many others do not yet have the ability to enact such regulations, making the importation and use of possibly tainted beef a health risk.

As a specialist in biochemistry, you have been asked to be part of a team to a country without regulatory legislation to help them understand BSE at a chemical level.

Task:

Design a multimedia presentation (e.g., PowerPoint, Keynote) for health workers on the biochemistry of BSE. Since these workers are unfamiliar with the basic biochemistry concepts necessary to understand how BSE occurs, you will need to include an overview of proteins.

Note: Please save presentation documents as *.ppt (PowerPoint) or *.pdf (Portable Document Format) files.When submitting a *.ppt file, please also submit a *.rtf or *.doc file of the text in order to check originality.

A. Explain how BSE occurs at a molecular level.

1. Create an original model of an essential amino acid with side chains.

Note: Include a photograph of your model in your attached presentation or as a separate attachment to this task.

2. Describe two chemical characteristics (i.e., reactivity, toxicity, flammability, or hydrophobicity) of the amino acid of which you created a model.

3. Create an original diagram or series of diagrams of the different levels of protein structure and label the primary, secondary, tertiary, and quaternary structures.

4. Demonstrate how a peptide bond is made through dehydration, using a relevant chemical equation with structural chemical formulas.

5. Demonstrate how a peptide bond is broken through hydrolysis, using a relevant chemical equation with structural chemical formulas.

6. Explain the four forces (bonds) that stabilize a protein’s three-dimensional structure at the tertiary level of protein structure.

7. Explain the role of protein misfolding and aggregation in BSE.

8. Explain the role of prions in BSE.

9. Explain the role of the chaperone protein in BSE.

B. Make recommendations for how this country that does not have regulations in place can decrease the risk of BSE infecting the food source.

Note: You are not explaining how the United States or the United Kingdom currently prevent BSE from infecting the food source.

C. When you use sources, include all in-text citations and references in APA format.