Questions 1 thru 10 are worth 4 points each, and question 11 is worth 10 points to total 50.
- Give the one and three letter abbreviations and R group classification for:
Alanine, Cysteine, Proline, Phenylalanine, Lysine, and Aspartate
- What bond type forms the primary protein or peptide structure? Where in the cell is this bond created?
- What are the advantages and disadvantages of HPLC as a technique for the separation of proteins and peptides? Name one other technique one might employ for separating and purifying proteins.
- Define the term PI as it relates to an amino acid.
- Which degradation procedure provides information about the primary structure of proteins? Explain this process in detail.
- What property of amino acids permits the measurement of protein concentration by UV light absorption?
- Can the amino acid methionine perform the same function as cysteine? ? Explain in detail why or why not.
- Explain why individual amino acids are soluble in water, and why not all peptides are water-soluble?
- Name a critical reagent used in electrophoresis to separate polypeptides based on their mass.
- How do number, sequence, and properties of amino acids in a protein affect its structure and function?
- Using the UF library resources online, locate the following journal article:
Touch V, Hayakawa S, and Saitoh K. (2004) Food Chemistry 84 (3): 421-428.
Questions 1 thru 10 are worth 3 points each, and 11 and 12 are worth 10 points each.
- Many weak interactions contribute to protein tertiary and quaternary structure. What causes peptide bonds themselves to be planar?
- Explain why Psi (Ïˆ) and Phi (Î¦) cannot both be zero.
- Compare and list the kinds of amino acids that may make up a polypeptide in a Î±-helix structure with those found in ÃŸ-sheet structures. What are the limitations of each of these conformations on the types of amino acid residues that may be incorporated?
- Explain which technique(s) you would use to determine if a protein has quaternary structure.
- List the conditions under which proteins become denatured and what bonds and interactions are disrupted during denaturation?
- Explain in detail whether or not a single amino acid could be an effective antigen and how a single amino acid substitution could affect ligand binding?
- Describe how an induced fit increases the strength of interaction between and antibody and an antigen.
- Name a protein that can exist in globular or filamentous form. Explain in detail the process by which one form is converted to the other.
- Describe the important protein – protein interactions between motor proteins. What other proteins are directly involved in the muscle contraction process?
- Briefly outline the mechanism by which heme is bound to globin? How could the cooperative binding of oxygen to hemoglobin be demonstrated graphically?
- Using your text and searching online, list what types of circumstances elicit chaperone proteins. Briefly describe the role of chaperonins and posit how they might be used therapeutically.
- Proteins comprising receptors can often transition across multiple conformational states.
Locate the following journal article.
Maelicke A, and Albuquerque E. (2000). European Journal of Pharmacology 393 (1-3): 165-170.