Science Homework Help

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 (ψ) and Phi (Φ) cannot both be zero.
• Compare and list the kinds of amino acids that may make up a polypeptide in a α-helix structure with those found in ß-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.

What property does the nicotinic acetylcholine receptor and the proposed treatment exhibit with regards to cooperative behavior?

What other specific example demonstrating this type of modulation of receptor activity is mentioned in the article?