Download Chemistry 160 Protein Structure Homework

Chemistry 160 Protein Structure Homework
1. Give three roles of proteins in an organism.
2. What are prosthetic groups?
3. What are glycoproteins and lipoproteins?
4. Describe the 4 levels of protein structure.
5. Describe 3 types of interactions that stabilize protein structure.
6. What drives protein folding?
7. Give two ways amino acid sequences are determined.
8. A small protein was cleaved in two separate experiments by chymotrypsin and by
trypsin. The chymotrypsin fragments were:
MAVKTMPW, ATF, AMERTPC, GMRTSSY
the trypsin fragments were:
ATFGMR, TPC, TSSYMAVK, TMPWAMER
What is the sequence of the protein?
9. Describe an α helix. Be sure to describe what stabilizes it and where the R groups are.
10. Why does proline not fit into an α helix.
11. Why do we not see amino acids of the same charge 4 residues apart in a helix.
12. Describe a β sheet. Be sure to describe what stabilizes it and where the R groups are.
13. What is tertiary structure? How is it determined?
14. What is supersecondary structure? Give some examples.
15. Show with structures, how a pH change can disrupt protein structure.
16. Discuss how proteins are purified.
17. What is specific activity? Briefly describe how it is determined.
18. Discuss what antibodies are and their use in affinity chromatography and ELISA.
Book Questions:
Pp. 120 - 121: 1, 5b, 5c, 7, 19, 20, 21, 25, 32, 41
Pp. 140 - 141: 11, 12, 15, 20, 29, 34, 37, 43