7. WHAT IS A PHOSPHODIESTER BOND? WHERE CAN IT BE FOUND? 8. GIVE AT LEAST 10 CARBOXYLIC ACIDS THAT HAVE A SIGNIFICANT ROLE IN BIOLOGICAL SYSTEMS AND/OR IN MEDICINE. 9. WHAT IS DECARBOXYLATION? CITE BIOLOGICAL PROCESSES WHICH INCLUDE DECARBOXYLATION.
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7. WHAT IS A PHOSPHODIESTER
BOND? WHERE CAN IT BE FOUND?
8. GIVE AT LEAST 10
HAVE A SIGNIFICANT ROLE IN BIOLOGICAL
SYSTEMS AND/OR IN MEDICINE.
9. WHAT IS DECARBOXYLATION? CITE BIOLOGICAL PROCESSES
WHICH INCLUDE DECARBOXYLATION.
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Solved in 2 steps
- 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?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…6. 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:
- 11. List 2 polysaccharides that provide structure and strength. What is interesting about the orientation/shape/bonding/architecture in these molecules?7. Hydrogen bonds are a crucial component of biomolecular structure and biomolecular interactions. In the following drawings, draw in several hydrogen bonds that are possible between atoms within the same molecule or between different molecules: A: Protein structure H₂C₁ #1 N-H N-C 0=C HR 1 N-H ORU 0=C N-HH-CR B: DNA base-pairing H H-N N-H N=C C-C H 0=C NIH C C=N HR 0=3₁ HR H-9-4 0-0 NIH N-H 0=C 0=0 RECH N-H N-H 0=8-₁ OH HR C: Plant cell wall (cellulose) CH₂OH H BỆNH O=C HA CH OH H CH₂OH ( он H HC-0 CH₂₂OH H OH 1 TH OH H IN HC- OH H CH₂OH CH₂₂OH O OH H C-CH H bH CH₂₂OH VA HS COK H ОН Biomolecules like DNA, proteins, and carbohydrates depend on hydrogen bonds to maintain their overall structure. However, each individual hydrogen bond is relatively weak. Using protein structure from the question above as an example, explain how to resolve the apparent contradiction between these two statements.Organic Molecules and Carbohydrates How many covalent bonds are formed by one carbon, and why? When a double covalent bond is formed, how many electrons are being shared? 3. Given a molecule that was drawn incorrectly, indicate which carbon does not have a sufficient number of bonds. 1. 2. Given a molecular formula (such as CH4) identify the molecule as inorganic or organic. 5. Given an organic molecule (molecular or structural formula) indicate whether the molecule is hydrophobic or hydrophilic and why. 6. Given two molecules, identify whether they are isomers of each other and explain why. 7. Explain the importance of functional groups. Be able to identify and name all functional groups. Define and explain the relationship of the following words: macromolecule, monomer, dimer and polymer. 9. Describe the chemical reactions of dehydration synthesis and hydrolysis in terms of what occurs, and what is accomplished. (Which can bond together monomers? Which splits a dimer or polymer into…
- 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. Make a series (at least 3) of drawings to show the three dehydration synthesis reactions that take place between the two Fatty Acids, the Phosphate Head and the Glycerol. Show the water molecules made. a) Label the following on the completed phospholipid: hydrophilic and hydrophobic parts of the molecule, fatty acids, phosphate group, and glycerol. b) Compare the structure of the phospholipid to that of a triglyceride. How are the two molecules Similar? How are they different? 2. Use the following vocabulary to label and draw a cell membrane: cytoplasm (cell lumen) extra-cellular fluid hydrophobic hydrophilic polar head non-polar tails a) How many O-H groups are there? And are the O-H areas of sucrose polar or non-polar? b) What is the term that is used to discuss how tightly or loosely an atom's nucleus has a hold of its valence electrons?6. Peptide bonds link many amino acids into chains of subunits that make polypeptides, or proteins. In the space below, or on a blank sheet of paper, draw the dehydration synthesis reaction showing the peptide bond that forms between two alanine (C3H;NO2) amino acids. Remember that all amino acids have an amino functional group at one end (N-terminal end) and a carboxyl functional group at the other end (C-terminal end). Also, alanine is an amino acid that has a CH3 off the middle ("R" group) carbon.
- 10. List 2 polysaccharides that are used for energy storage. What is interesting about the orientation/shape/bonding/architecture in these molecules?1. a. Draw the following pentapeptide: lysine-leucine-aspartate-threonine-phenylalanine b. Label the amino and carboxyl terminus of your peptide c. Label each amino acid residue with one and three letter abbreviations d. Label the alpha carbons e. Label the bonds around which phi and psi rotational angles occur f. Which amino acid in this chain is most likely to be phosphorylated? Which amino acid is most likely to be acetylated?1. What is the chemical formula for palmitic acid and oleic acid? Which one is a saturated fat and which one is an unsaturated fat? How do you know? 2. What functional groups are involved in dehydration synthesis reactions to form a triglyceride? What is the waste product? 3. Compare the overall acidity of the molecules before and after the formation of a triglyceride. Proteins 1. What gives each amino R group its key characteristics to make it polar, non-polar, or ionic? 2. What functional groups are involved in dehydration synthesis? 3. How might the solubility of peptides be influenced by the size of the peptides? How might the R group of the amino acid influence it? 4. Would you consider the formation of a peptide bond to be an example of a neutralization reaction? Explain your reasoning.