GRT Task 2
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BIOCHEMISTRY

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.

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 import and use of possibly tainted beef a health risk.

Scenario:

As a specialist in biochemistry, you have been asked to be part of a team that will assist a country without regulatory legislation. You will help the other workers in understanding BSE at a chemical level. Because these workers are unfamiliar with the basic biochemistry concepts necessary to understand how BSE occurs, you will need to include an overview of proteins.

Requirements:

Design either a multimedia presentation (e.g., PowerPoint, Keynote, Google Presentation) or a report (e.g., Microsoft Word, Google Document) for health workers on the biochemistry of BSE by doing the following:

Note: You are not limited to a specific length, but suggested lengths are 10–15 slides for a presentation and 3–5 pages for a report.

Note: Please save submission documents as *.ppt, *.pptx (PowerPoint), *.key (Keynote), *.doc, *.docx (Word) or *.pdf (Portable Document Format) files. If you are using Google Presentations or Documents you must save the file in *.pdf format and upload the *.pdf file.

A. Create an original model of an essential amino acid that shows all atoms and bonds in both the backbone and the side chain.

Note: Take a picture of your completed model as evidence that you created it. You can include the picture as part of your presentation or report, or you can upload it in Taskstream as a separate attachment.

1. Describe two characteristics (e.g., reactivity, hydrophobicity, how it affects the structure or functions of a protein) for the amino acid model you created in part A.

B. Create an original diagram, or series of simple diagrams, of the different levels of protein structure.

1. Label the primary, secondary, tertiary, and quaternary structures in your diagram(s).

C. Create an original diagram, or series of simple diagrams, that demonstrates how a peptide bond is made through dehydration, using a complete chemical equation that includes the following components:

• chemical structures of all reactants

• an arrow indicating the direction of the reaction

• the chemical structures of all products

D. Create an original diagram, or series of simple diagrams, that demonstrates how a peptide bond is broken through hydrolysis, using a complete chemical equation that includes the following components:

• the chemical structures of all reactants

• an arrow indicating the direction of the reaction</font

• the chemical structures of all products

E. Explain the four forces (i.e., bonds or interactions) that stabilize a protein’s structure at the tertiary level of protein structure.

F. Explain how bovine spongiform encephalopathy (BSE) occurs at a molecular level by doing the following:

1. Explain the role of protein misfolding and aggregation in BS, including the following points:

• the name of the protein that is misfolding

• why the protein is misfolding

• why there is aggregation

• what structures the aggregated proteins form

• how this process leads to the symptoms of BSE

2. Explain the role of prions in BSE, including the following points:

• what a prion is

• the name of the prion in BSE

• how prions lead to the disease

3. Explain the role of the chaperone protein in BSE, including the following points:

• how chaperones normally act in the cell

• the name of the specific protein that acts as a chaperone in BSE

• how the protein that acts as a chaperone is different from typical chaperone proteins

4. Recommend ways that a country that does not have regulations in place can decrease the risk of BSE infecting the food source, based on your understanding of BSE and how it spreads (e.g., feeding practices, animal disposal).

Note: You are not explaining how the United States or the United Kingdom currently prevent BSE from infecting the food source. Your recommendations should be simple ones that any country could implement.

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

Note: For definitions of terms commonly used in the rubric, see the Rubric Terms web link included in the Evaluation Procedures section.

Note: When using sources to support ideas and elements in an assessment, the submission MUST include APA formatted in-text citations with a corresponding reference list for any direct quotes or paraphrasing. It is not necessary to list sources that were consulted if they have not been quoted or paraphrased in the text of the assessment.

Note: No more than a combined total of 30% of a submission can be directly quoted or closely paraphrased from sources, even if cited correctly. For tips on using APA style, please refer to the APA Handout web link included in the General Instructions section.
Web Links:
1. Rubric Terms link opens in new window

Click to Show/Hide MethodEvaluation Method
A rubric is used in this Evaluation.
Name of rubric: GRT Task 2 (0814) [View rubric link opens in new window]
Final scoring method: Evaluator marks as “Meets Requirement/Does not Meet Requirement”