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- 5.) The side chain (R group) of tyrosine can hydrogen bond to water in two different ways. Use the image of the tyrosine R group below and draw these potential hydrogen bonds with water.2. a. In the following diagram of a portion of a protein, label the types of interactions that are shown. b. What level of protein structure are these interactions producing? b. CH CH3 CH3 Polypeptide backbone CH2 H3C H3Ç 10 CH С—ОН - CH,-S-S-CH,- а. CH2 с. -CH,-CH,-CH2-CH2-NH 0-C-CH2- d.1. Hypoxanthine is an unusual nitrogenous base that can be formed from adenosine; it is not normally found in nucleic acids. Hypoxanthine has a single ionizable group with a pKa of 8.7. If you dissolved hypoxanthine in an aqueous solution at pH 7.0, would this ionizable group be protonated or deprotonated?
- 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…1. It is important that you are familiar with the bonding within major macromolecules - carbohydrate, protein, lipid, nucleic acid. Name the key bond involved with the formation of the following: maltose, glutathione, triglyceride, and DNA.4. Each diagram in Figure 2 below shows one level of organization of a protein. Identify each level and describe it. CA ITA (a) (b) 0 hydrogen co CH₂ bond H-0 (c) -0, 0 lonic bond C-OH H₂C H₂C CH-CH₂ amino acids -hydrophobic interactions disulfide bridge Figure 2 5. Hemoglobin is made up of four polypeptides, but also require a beme group
- 1. Draw a circle around and give the name of each functional group in the following twomolecules. (Note: each line represents a covalent bond. If no atom is shown, assume there’s a carbon there.)2. Two amino acids are shown below. Name them in the blanks, and then draw the structure of the dipeptide they would form if a peptide bond connected them (in the order shown.) Draw the dipeptide as a Zwitterion, and name it in the blank. H3N-CH- CH-C-O CH3 + + H3N-CH₂-C O1.What reactive groups are involved in the formation of a peptide bond?2.A molecule of what substance must be removed in order to form a peptide bond?
- 3. In a solution of alanine molecules, approximately what fraction of the alanine will exist as the zwitterion at pH of 2.34? What would be the average net charge of a solution of alanine molecules at pH 2.34? 50% will exist as the zwitterion and 50% will exist as the fully protonated (COOH/ NH3+) form. The average net charge of this solution would be +0.5.6. How are amino acids linked together in a protein molecule? Write the general structure of the tripeptide lys-phe-meth. Show their peptide bonds. Illustration: Label the amino acids.1. An oligosaccharide is a repeating unit of a-D-galactopyranosyl- (a-1- 3)-allopyranoside. Each of the disaccharide unit is linked via B-1-->4 glycosidic bond. Identify and draw the molecular structure. Identify and draw the structure. The oligosaccharide has 10 monosaccharide residue a. Upon the action of alpha-glycosidase, identify and draw all the possible products. b. What is the L-isomer of the Fisher projection of one epimer of D-allopyronoside. Draw the structure. Why is this an epimer of the monosaccharide? c. Is this saccharide a good substrate for glycolysis? Why or why not?