Name ________________________________________
Chapter 3: Carbon and the Molecular Diversity of Life
3.1
1. Define what organic chemistry is.
2. What makes a molecule a macromolecule?
3. Discuss why carbon is the backbone of living things.
4. Identify and discuss the 4 ways carbon skeletons may vary.
5. Draw a model of each of the following functional groups found in organic compounds. Indicate where it
what it would be found in
a. Hydroxyl group
b. Carboxyl group
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c. Amino group
d. Phosphate group
e. Sulfhydryl group
f. Methyl group
6. Discuss the importance of the Phosphate functional group in ATP molecules. Draw a diagram to show
this.
3.2: Carbon and the Molecular Diversity of Life
1. Identify the 3 classes of Macromolecules.
2. What makes a macromolecule considered to be a macromolecule?
3. Differentiate between a polymer and a monomer.
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4. Explain how enzymes are involved in polymerization (dehydration synthesis) and hydrolysis.
5. Identify the diagrams below, labeling them appropriately.
6. Give an example of hydrolysis in us and explain its necessity.
7. Explain why there is such a tremendous diversity of macromolecules in living systems.
8. What are carbohydrates?
9. Identify the monomer of all carbohydrates and their molecular formula.
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10. Identify each of the monosaccharides shown below, with formula and common name
11. What happens to the above when in an aqueous solution?
12. What is the main purpose for monosaccharides?
13. What happens to excess monosaccharides that aren’t used immediately?
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14. Circle where dehydration synthesis will occur and then color the 1-2 glycosidic linkage bond. (please
note that the top set of sugars and bottom set do not go together.)
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15. Identify the three types of disaccharides and give an example of each.
16. What is the purpose for polysaccharide and give a few examples of them.
17. Label each of the polysaccharides shown below.
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18. What is glycogen and where is it stored?
19. Why is cellulose referred to as a structural polysaccharide while others function as stored energy?
20. What is the problem with the 1-4 β glycosidic bonds of cellulose when ingested by many animals?
21. Another structural polysaccharide is chitin. Where is it found?
3.4: Lipids
1. Explain why lipids are hydrophobic.
2. Identify the 4 types of lipids.
3. What are the monomers (smaller units) of all fats?
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4. What functional groups are found in the two molecules above?
5. What is a triglyceride?
6. Label the ester linkage in the diagram below and determine if the triglyceride is saturated, unsaturated or
a polyunsaturated fat.
7. Give an explanation to your answer for 6.
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8. Give the characteristics of the saturated and unsaturated fats shown below.
9. As a result of the double bond in the unsaturated fatty acid hydrocarbon chain, what occurs and what
does this do to the fat?
10. What is the main purpose for lipids in the diets of living things?
11. Explain how the form of the cell membrane fits perfectly with the function of the cell membrane.
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12. Label the hydrophobic and hydrophilic parts of the phosopholipids below in all 4 diagrams..
13. How is steroid structure so different from other lipids?
14. What differentiates the different types of steroids?
15. What is the name of this necessary steroid and what is its purpose? What might it lead to?
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3.5: Proteins
1. What percent of the dry mass of most cells is protein?_________
2. Give 8 functions for proteins in living organisms
3. What is an enzyme and what is its function?
4. Proteins are polypeptides of _________________
5. Label the parts of the monomer of proteins in the diagram below.
6. What determines the properties of the amino acid?
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7. What two functional groups are common to all amino acids? Draw them.
8. Circle the peptide bond(s). Color the amino groups blue & the carboxyl groups red.
9. Discuss what determines the structure of a polypeptide?
10. Now discuss how the form of the specific protein determines its function. Give 2 examples.
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11. Label each of the diagrams below showing the levels of protein structure.
12. What causes the folding or pleating patterns in the secondary structure?
13. What is the main cause of the shape of the tertiary structure?
14. Give 2 examples of a protein which have the quaternary structure.
15. Examine figure 3.22 in your book and determine what causes the shape of a sickled red blood cell.
16. What conditions could denature a protein’s structure?
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Section 3.6: Nucleic Acids
1. What are genes made up of and what do they do?
2. What are 2 functions of DNA?
3. Very simply, go through Protein Synthesis starting at the gene on DNA.
4. Identify and label the structure below.
5. Identify each of the nitrogenous bases and then classify them as either a purine or a pyrimidine.
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6. Differentiate between the sugars in DNA and RNA. What is the difference?
7. Now label the DNA strand below with an S for sugar, N for Nitrogen base or a P for Phosphate groups.
Also label the 5` end and the 3` end.
8. So what is the name of this special covalent bond that links the sugar and phosphate groups together?
9. Where exactly is the genetic code on a DNA strand?
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10. Explain what is meant by the DNA strands being antiparallel.
11. Discuss complementary base pairing with DNA and RNA.
12. How can DNA be used as a tape measure for evolution?
13. Look at the bases in the diagram below. Based on this evidence, which species are we more closely and
most distantly related to?
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