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BIO 251 - Cell & Molecular Bio-Proteins

1. Demonstrate an understanding of amino acid chemistry.
   1. Memorize the structure of the twenty amino acids.
   2. Categorize the amino acids according to the properties of the side chains.
   3. Generally describe amino acid synthesis in the cell.
2. Give a detailed explanation of protein structure.
   1. Draw and list the properties of the peptide bond.
   2. Draw the structure of the twenty common amino acids and recognize molecular models of each.
   3. Describe the four structural levels of proteins.
   4. Lis and describe the forces involved in protein folding and conformation.
   5. Explain the differences between a fibrous protein and a globular protein.
   6. Correlate protein folding with protein synthesis.
3. Demonstrate a general understanding of protein function within the cell.
   1. List functional roles of proteins in living systems.
   2. Explain how proteins bind and interact with other molecules.
4. Discuss methods used in the characterization and purification of proteins.
   1. Describe common methods used in protein purification including differential centrifugation, dialysis, salting out, liquid chromatography (size exclusion
   2. Discuss methods for characterizing proteins including ultracentrifugation, polyacrylamide gel electrophoresis (PAGE), SDS-PAGE, isoelectric focusing, UV absorption spectroscopy, X-ray diffraction and crystallography.
   3. Explain how proteins can be sequenced and digested.
5. Provide a detailed description of processes involved in protein synthesis.
   1. Describe the structures of mRNA, rRNA and tRNA and their roles in translation.
   2. Define degenerate and wobble as they relate to translation.
   3. Describe how proteins are targeted and modified within the cell and explain the importance of these events.
   4. Discuss how translation can be regulated by the cell.
6. Discuss the mechanism and dynamics of catalytic proteins.
   1. Draw and discuss a simple model of an enzyme catalyzed reaction.
   2. Describe how processes are accomplished through metabolic pathways.
   3. Explain how enzyme activity can be regulated by feedback inhibition.
   4. List key features of the active site.
   5. Memorize the Michaelis-Menton equation and explain how it relates to a saturation profile of an enzyme.
   6. Explain the significance of Km and Vmax values.
   7. Compare and contrast competitive, non-competitive and uncompetitive types of reversible inhibition.
   8. Use a graph to describe the effects of temperature and pH on enzyme activity.
   9. Discuss the importance of enzymes in biotechnology applications.
7. Discuss the roles of immunoproteins and how they can be used as tools in the laboratory.
   1. Explain how antibodies are made in vivo.
   2. Draw and label a generalized model of an antibody.
   3. Describe the mechanism of action of antibodies.
   4. Contrast monoclonal versus polyclonal antibodies.
   5. Discuss the importance of antibodies in biotechnology applications.
   6. Draw models demonstrating enzyme-linked immunosorbent assays
8. Provide an explanation for differential proteins expression within the cell.
   1. List and discuss cellular stimuli that may alter the protein content of cells.
   2. Relate differential protein expression to cell specialization.
   3. Discuss stress responses of some cell types.
9. Purify a protein.
   1. Store and handle enzymes using appropriate methods.
   2. Assay samples for total protein content.
   3. Prepare cell extracts and sub-cellular fractions.
   4. Separate proteins using chromatographic methods such as size exclusion, ion exchange and affinity liquid chromatography.
10. Characterize enzyme activity.
    1. Calculate enzyme activity units.
    2. Detect activity using a colorimetric enzyme assay.
    3. Manipulate kinetic data using appropriate software.
    4. Describe the differences of various effectors on enzyme rate.
11. Perform a variety of immunoassays including
    1. PAGE
    2. SDS-PAGE
    3. Western blot
    4. ELISA
12. Perform two dimensional gel electrophoresis.
    1. Prepare a sample for isoelectric focusing.
    2. Separate proteins in a sample using isoelectric focusing.
    3. Prepare a sample for separation in the second dimension.
    4. Set up and run a gel for separation of proteins by molecular weight (second dimension).
    5. Analyze 2-D gel images using appropriate imaging software.

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