Download AP Biology

AP Biology
Ch. 5 Learning Team Questions Part 1
Name_______________________
Polymer Principle and Carbohydrates
1. What is a polymer and what are the building blocks of polymers called? Give an
example of each?
2. Explain the process of dehydration synthesis. Why is hydrolysis the opposite of
dehydration synthesis?
3. There is a tremendous variety of macromolecules found in living organisms. What
is the basis for such diversity in life’s polymers?
4. What is the main structural difference between an aldose and a ketose? Why are
these terms useful in classifying monosaccharides?
5. Why is it inaccurate to draw glucose with a linear carbon skeleton?
6. Define glycosidic linkage. Name 3 major disaccharides and the monosaccharides
that compose each.
7. Describe how the starch molecules amylose and amylopectin are formed. What is
the general shape of a starch molecule?
8. What is glycogen?
9. What is the difference between alpha glucose and beta glucose?
10. Describe the three dimensional structure of cellulose and how this structure
applies to the function of cellulose.
AP Biology
Ch. 5 Learning Team Questions Part 2
Name_______________________
Proteins
11. Describe the structure of an amino acid. What is the alpha carbon? Do any of the
amino acids contain alpha carbons that are not asymmetric?
12. What is an R group? Discuss the various properties that the R group (side chains)
possess. Give an example of each type of amino acid.
13. Describe the process of polymerization of amino acids. What is a peptide bond?
What is located at the each end of a polypeptide chain?
14. Explain why the term polypeptide is not synonymous with protein. What
ultimately determines the three-dimensional structure of a protein?
15. Is there a relationship between the structure of a protein and its function within a
cell? Give a specific example.
16. How is the specific function of a protein an emergent property resulting from the
order of the amino acids in a polypeptide chain
17. What is the primary structure of a protein? What determines the specific order of
amino acids in a polypeptide chain like the enzyme lysozyme?
18. Discuss what might happen if the primary structure of a polypeptide chain is
changed even slightly. Describe the example of normal hemoglobin verses sicklecell hemoglobin.
19. Discuss the work that Frederick Sanger did to figure out the primary structure of
the insulin hormone
20. What type of bond contributes to the secondary structure of a protein? Which
parts of the amino acid are involved? How are they involved?
21. What are the two possible secondary structures of proteins? Briefly describe each
structure and give examples of proteins that illustrate these structures.
22. What part of an amino acid is directly involved in the tertiary structure of a
protein? Explain how hydrophobic interactions work. What is the relationship
between hydrophobic interactions and van der Waals interactions?
23. What role do sulfhydryl groups (-SH) play in the tertiary structure of a protein?
Which amino acids contain sulfhydryl groups?
24. Discuss situations of tertiary structure that would involve hydrogen bonds and
ionic bonds. Be specific.
25. Define quaternary protein structure. Explain how quaternary structure contributes
to the macromolecules collagen and hemoglobin.