3. Hydrogen Bonds a. Draw 4 additional water molecules (each with red polar covalent bonds) attached to 1 central water molecule. b. Indicate which bonds are hydrogen bonds by using a blue dashed line (- - - -) for each of those bonds.
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- 1. Polar Covalent Bonds a. Draw one water molecule. b. Indicate which bonds are polar covalent bonds by using a solid red line for each of those bonds. c. Label the partial charges.8) Define the following terms: a. Hydrophobic b. Hydrophillic 9) Describe the composition of a phospholipid and its relationship with water. Be specific about how the different parts of a phospholipid interact with water.1. a. Explain why the melting point of palmitic acid (16 carbons, no double bonds) is slightly lower thanthat of stearic acid (18 carbons, no double bonds). Explain why the melting point of oleic acid (18carbons, one double bond) is lower than that of stearic acid b. A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.
- 1. Complete the given table below. What properties do each of the following R groups have? Hydrophilic or |hydrophobic Basic, acidic, or Polar or nonpolar R Group neutral CH, CH3 b. CH2 CH2 CH2 CH2 NH5 d. CH2 он6. Identify the following functional groups AND provide an example of one biomolecule containing that functional group. A B C D E Chemical formula - PO, - COH -OH -COOH -NH₂ Structural formula O -O-P-0° 0= 0- N H -OH C=O OH H H Example: Example: Example: Example: Example: Riomolecules:Below are two amino acids at physiological pH. Number labels are for part c. Answer the following questions about the side chains of these amino acids. H C. H;N* 2 CH2 A H H3N* C 3 CH2 В 4он В a. Which amino acid has a polar side chain? b. Which amino acid is more soluble in water? B c. Select the atom that serves as the hydrogen bond donor in the amino acid's R group.
- 1. List the names of the 9 hydrophobic "R" groups. a) What are the two most common atoms across these 9 "R" groups? b) Look at the hydrophilic side chains. Besides carbon & hydrogen, what are the two the most common atoms in this group? 2. On the chart, locate the two acidic side chains. They both have a carboxylic acid functional group. What charge do these side chains have? a) On the chart, locate the two basic side chains. They both have an amino functional group. What charge do these side chains have? b) Locate cysteine on the chemical properties circle. What atom is found in this side chain that is not found in most of the others (except methionine)?Proteins and Amino Acids A. Acid-base properties of proteins: 1. Data a. Color phenolphthalein-NaOH solution -before adding casein : colorless - after adding casein :colorless cloudy b. Color of methyl orange-HCl solution - before adding casein :Blue - after adding casein : Pink 2. Why did the solutions change color? 3. Which property of proteins is illustrated by the above? 4. Why as methyl orange used in place of phenolphthalein in the second part of this procedure? B. Isoelectric point of casein: 1. Data Initial pH of milk Final pH of milk 2. What is the isoelectric point of casein? C. Denaturation of proteins: A. pH 1. Observations: a. Tube no. 1: concentrated HCI b. Tube No. 2: concentrated HNO, c. Tube No. 2: concentrated H,SO, 2. Which structure(s) of the protein were disrupted in this procedure?6. The [a] of cheatalotic acid is + 10°. The structure shown below was thought to be correct. Answer for Part b HO, COOH H, HO OH Cheatalotic Acid Incorrect Structure a) Why is the structure shown incorrect? b) Propose a cture of cheatalotic acid that can possibly be correct, assuming atom connectivity is correc
- 6. b. Draw a box around the disulfide bridge in oxytocin, if present, or write "none". 7. Mark each peptide bond in oxytocin by making the corresponding line in the structure thicker or marking it with a different color. The first one is shown for you as an example (in dark orange). 8. Number the central carbon of each amino acid in oxytocin by pointing a small arrow to it or by circling the corresponding vertex in the image. Numbers 1 and 2 indicate the central carbons of the first and second amino acids of oxytocin, and are shown for you as an example. 9. Fill out the following table, listing amino acids that make up oxytocin in order, from the N terminus to the C terminus, characterizing each amino acid by the properties of its R group (side chains), and briefly indicating the reasoning for the characterization. You may consult amino acid groupings by category in the slides (or the textbook, p.49), but you must explain the reasoning for each in your own words. CO 1 AA# Abbre- Full…A. A solution of amino acid having carboxylic side chain was titrated against NaOH. If the initial pH of the solution was 2.8. Describe the state of the functional groups of the amino acid at the initial pH and at 10.5 B. Briefly explain how you will separate amino acid mixture using the change difference between amino acids. C.A given glycine solution was titrated against NaOH and pH of the final solution was 4.8. Given that pKa1 and pKa2 of the glycine are 2.34 and 9.60 respectivel. Calculate the concentration of the dissociated amino acid in terms of the undissociated amino acid. If [x] and [y] are the concentration of dissociated and undissociated amino acid respectively.1c) Suppose you increased the pH of the biotin solution from 7.0 to 9.0 -what would happen to the ionizable group on a molecule of biotin as the pH shifted from 7.0 to 9.0?