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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
Chapters 2, 3.1, and 3.2
Review of Chemistry and Biochemistry Topics
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1. Contrast the terms atom and element.
2. State six elements essential to life that make up 95% of living matter.
3. Describe the structure of an atom - label the diagram below and define the terms that you label.
4. Contrast the terms atomic mass and atomic number.
5. What is the difference between the terms atomic mass and atomic weight?
6. Given the atomic number and mass number of an atom, how would you determine the number of
neutrons?
7. What is an isotope and what is ‘special’ about radioactive isotopes?
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
8. What determines interactions between atoms? How are valence electrons important? Look at
Figure 2.1 and predict the number of covalent bonds each atoms is capable of forming. Explain
WHY in terms of the octet rule.
9. Distinguish ionic and covalent bonds.
10. Define electronegativity and explain how it influences the formation of chemical bonds.
11. Distinguish among nonpolar covalent and polar covalent bonds.
12. What is the difference between a structural and molecular formula?
13. What are some types of structural models used to represent the bonding/shape of a molecule?
14. Explain how the type of bonding involved affects the final shape of the molecule.
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
15. Describe the formation of a hydrogen bond and explain how it differs from a covalent or ionic bond.
16. Distinguish between the terms hydrophilic and hydrophobic. What determines is a molecule will be
hydrophilic or hydrophobic overall?
17. Compare and contrast van der Waals interactions with other types of chemical bonding.
18. Rank the types of chemical bonding in terms of energy, from least to greatest.
19. Based on the reading, what is an example, in a living system, of how molecular shape is critical.
20. Why is water considered a polar molecule?
21. Draw two water molecules in a way that illustrates a hydrogen bond.
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
22. Distinguish between heat and temperature.
23. Define: (you may need to use another source for these terms)
a. Calorie
b. Specific heat (heat capacity)
c. Heat of vaporization
d. Heat of fusion
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
24. Below is a heating/cooling curve for water.
Label the points at which water would be a gas,
liquid, and solid. Also indicate the transition
points and which corresponds to the heat of
vaporization and heat of fusion). What is so
special about the curve during phase transition?
25. For each of the properties of water, briefly define the property and then explain how water’s polar
nature and polar covalent bonds contribute to the special property. Include an example in nature of
each property also.
a. High heat capacity
b. High heat of vaporization/fusion
c. Evaporative cooling
d. Cohesion
e. Adhesion
f.
Surface tension
26. What is special about water and density?
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
27. Define the following terms:
a. Solute
b. Solvent
c. Aqueous solution
d. Hydrophilic
e. Hydrophobic
f.
Hydration shell
28. Label the diagram below to demonstrate the dissociation of the water molecule and then relate this
diagram to pH (be sure to give the equation for pH).
29. What defines an acid and a base?
30. Distinguish between a strong acid/base and a weak acid/base.
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
31. What are the components of a buffer? Write and explain the carbonic acid buffer system in human
blood. You will see this equation again!
32. How do buffers illustrate the law of mass action?
33. Why are apparently small changes in pH so important in biology?
1. Compare and contrast inorganic and organic molecules
2. What is special about carbon that makes it the central atom in the chemistry of life?
3. Create a table below. After each functional group - draw the structure, name the compound, write
an example, and note the functional properties. (Doesn’t this look like great exam material?)
a. Hydroxyl
b. Carbonyl (aldehyde and ketone)
c. Carboxyl
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
d. Amino
e. Sulfhydryl
f.
Phosphate
4. With each of the above functional groups, what type of bonding interactions could each one take
part in?
5. Which functional groups have the ability to function as acids or bases?
6. What are the four major classes of macromolecules in cells?
7. What type of chemical reactions are used to make/break macromolecules? Diagram each reaction
below.
CARBOHYDRATES
8. What is the general formula for a carbohydrate?
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
9. What are the major roles of carbohydrates?
10. Describe the structure of a typical monosaccharide such as glucose.
11. Differentiate between hexose and pentose sugars.
12. Describe the structure of a typical disaccharide such as sucrose. Write out a condensation reaction
between glucose molecules, and explain hydrolysis. (What type of linkage is formed?)
13. Define the properties/composition of the four major polysaccharides found in cells.
a. Starch / Glycogen
b. Cellulose
14. How does the orientation of the linkage differ between starch (maltose) and cellulose (cellobiose)?
(see Figure 2.10)
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
LIPIDS
15. A fatty acid is technically composed of C, H, and O, just like carbohydrates – however they have
quite different chemical and physical properties. Explain why.
16. What are the various roles of lipids?
17. Diagram the synthesis of a triglyceride and a phospholipid molecule. Circle and label all the
functional groups involved in this process – what type of linkage is formed? Point out the polar and
nonpolar ends of the phospholipids – also identify the hydrophobic and hydrophilic ends of this
molecule.
18. Explain the difference between a saturated and unsaturated fatty acid. List some unique emergent
properties that are a consequence of these structural differences.
19. Differentiate between a fatty acid, triglyceride and phospholipid.
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
20. Sketch a phospholipid below. What is the significance of a polar head and non-polar tails in a
phospholipids? (Use the term amphipathic.)
21. What is the basic structure of a steroid? List the three steroids described in your text and their
function(s).
CHEMICAL REACTIONS AND ENERGY
34. Explain what happens when a chemical reaction occurs.
1. Define the following terms:
a. Energy
b. Kinetic energy
c. Potential energy
2. Define:
a. Metabolism
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
b. Anabolism
c. Catabolism
3. Why are catabolic and anabolic reactions often linked in living organisms?
First Law
State the Laws of Thermodynamics:
Second Law
4. What is free energy?
CHAPTER 3.1 -- NUCLEIC ACIDS
22. Diagram an individual nucleotide, identify the 5-carbon sugar, the phosphate group and the
nitrogenous base. Describe how these monomers are linked together to form a nucleic acid. What
type of linkage is this?
23. Distinguish between a pyrimidine and a purine. How do purines and pyrimidines pair up in
complementary base pairing?
24. Summarize the functions of nucleic acids.
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
25. Distinguish between RNA and DNA (both in terms of structure and function).
26. List the functions of nucleotides like ATP, GTP, and cAMP.
27. What is so special about the triphosphate group on ATP?
CHAPTER 3.2 PROTEINS
28. Identify the alpha-carbon, the carboxyl group, the amino group, and the R group of an amino acid.
29. Explain how amino acids may be grouped according to the physical and chemical properties of the
side chains. Be sure to explain the significance of the following amino acids: cysteine, glutamic
acid, lysine, arginine, aspartic acid, and histidine.
30. Identify a peptide bond and explain how it is formed.
31. Explain what determines protein conformation and why it is important.
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
32. Define primary structure.
33. Describe the two types of secondary protein structure, and explain the role of hydrogen bonds in
maintaining the structure.
34. Define tertiary structure. Explain how weak interactions and disulfide bridges contribute to tertiary
protein structure.
35. Using hemoglobin as an example, describe quaternary protein structure.
36. Define denaturation and explain how proteins may be denatured. (Why are proteins so sensitive to
changes in temperature and pH.)
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AP Biology
Chemistry Review for Course
Reading Guide – Chapters 2 – 3.1 and 3.2
37. Summarize the types of chemical bonding involved in each level of protein structure.
38. Discuss several environmental conditions that may affect protein structure. What is the specific
effect of each on bonding interactions that generally maintain protein structure?
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