Reading guide
AP Study guide
Chapter 5 pages 68-89
Biology by Campbell and Reece 7th edition
Directions: All answers and diagrams must be answered in your interactive notebook. All diagrams
MUST be drawn neatly and the use of color is encouraged. Diagrams should be labeled clearly where
appropriate. All diagrams and definitions as well as sentence completions must be answered in full
sentences.
1. List the four main classes of large biological molecules
2. Distinguish between a polymer and a monomer.
3. Describe the process that connects monomers. Draw the diagram found on page 69 of this
process. Be sure to clearly label it.
4. Describe the process that breaks down polymers. Draw the diagram found on page 69 of this
process. Be sure to clearly label it.
5. When two monomers are joined a molecule of ________is always removed.
6. What are the monomers of carbohydrates?
7. What is the function of a carbohydrate?
8. Draw an abbreviated ring structure of a sugar molecule as shown on page 71. Circle the number
2 carbon.
9. Give an example of two structural polysaccharides.
10. Lipids are a class of large biological molecules that do not have polymers. It’s just one very large
molecule? Carefully draw a triacylglycerol molecule like one that is found on page 75.
11. What characteristic do all lipids share?
12. One of the most important fats that we learn in biology is the phospholipid. Describe how a
phospholipid shows ambivalent behavior toward water (pg. 77)
13. Table 5.1 is an important description of the function of proteins. Choose five proteins and
summarize each type. Do this by drawing a table into your interactive notebook.
14. Explain the sketch on page 78 (Figure 5.16) HINT: use the blue print numbers 1, 2, 3 and 4.
15. The monomer, or basic unit of a protein is an amino acid; draw a sketch of an amino acid
9Figure 5.17) into your notebook. Label the carboxyl group, the amine group, the R group and
the methyl group.
16. Define the following terms: peptide bond, dipeptide, and polypeptide.
17. There are four levels of protein structure. Refer to figure 5.20 and summarize each level in the
following table. This table MUST be created and placed in your interactive notebook.
Level of Protein Structure
Explanation
Example
o
Primary (1 )
Secondary (2o)
Alpha helix
Beta Pleated sheet
Tertiary (3o)
Quaternary (4o)
18. In the area under your table, draw an example of each level of protein structure.
19. Looking at the tertiary structure on page 83, make a list of the five types of bonding that is
found in this protein structure.
20. Explain how a change in the protein structure affects the ability of people with sickle cell anemia
to carry oxygen.
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26.
Define the term denaturation. Explain three ways that a protein can be denatured.
Draw and label a nucleotide in your notebook such as is found in Figure 5.26.
Explain why we consider the double helix “antiparallel?”
What two molecules make up the sides of the double helix?
Which molecules make up the “rungs” of the double helix?
Match the DNA strand below to its compliment.
5’AGTCCGGAT3’
27. Make a chart in your notebook for the structure and function of each of the four large biological
molecules: Carbohydrates, Proteins, Lipids and Nucleic acids. Make your chart in this way.
28. Place the name and definition in the first column, a diagram of the molecule in the second
column, examples in the third column and its function in the fourth.