In: Chemistry
1. What are some of the functions of lipids in the body?
2. Draw an example of each type of the following lipids: a. Fatty acid (saturated and unsaturated) b. Prostaglandin c. Wax d. Triacylglycerol (Fat and oil) e. Glycerophospholipid f. Sphingolipid g. Steroid
3. How do saturated and unsaturated fatty acids differ? What factor(s) affect the difference(s) in melting points of saturated and unsaturated fatty acids of the same carbon chain?
4. Draw the condensed structural formula for the ester formed from 3 moles of stearic acid and glycerol.
5. Draw the structural formula for the product of the hydrogenation of the following triacylglycerol:
6. Identify the following features of the phospholipid below: a. Is the phospholipid formed form glycerol or sphingosine? b. What are the fatty acids? c. What type of bond connects the fatty acid? d. What is the amino alcohol? e. What type of bond connects the amino alcohol?
7. What is the major function of cholesterol in the body?
8. What is the function of bile salts in digestion?
9. What is the function of the lipid bilayer?
10.Identify the type of transport described by each of the following: a. an ion moves from low to high concentration in the cell. b. carbon dioxide moves through a cell membrane. Amino Acids and Proteins 1. What functional groups are found in all amino acids? 2. Draw the structure of each amino acid below at low pH (pH = 1), pH = 7.4 and high pH (pH = 14) and classify it as polar or nonpolar. If polar, indicate if the R group is neutral, acidic or basic. Indicate if each is hydrophobic or hydrophilic. a. lysine b. proline c. valine d. tyrosine 3. Define the following: a. Zwitterion b. Isoelectric point 4. Draw the condensed structural formulas for each of the following peptides and give the three-letter and/or one-letter abbreviations: a. prolylaspartate b. threonylleucine c. methionylglutaminyllysine d. histidylglycylglutamylisoleucine 5. What is the difference in hydrogen bonding between and alpha-helix and a beta-sheet? 6. Indicate whether each of the following statements describes primary, secondary, tertiary or quaternary protein structure: a. Hydrophobic R groups seeking a nonpolar environment move toward the inside of the folded protein. b. An active protein contains four tertiary subunits c. Valine replaces glutamate in the beta-chain. d. Protein chains of collagen form a triple helix. 7. What structural level of protein is affected by hydrolysis? (primary, secondary, tertiary and/or quaternary) 8. Note the 5 types of denaturation and an example of each. 9. How does denaturation of a protein differ from its hydrolysis?