Reading Guide: Pratt and Cornely, Chapter 4, pp 104-114
1. How are proteins denatured?
2. All the information required for a protein to fold is contained in _____.
3. Name two types of covalent modification that might occur in protein processing.
4. Typically, when a protein is misfolded, what two possible fates awaits it? What third
possibility leads to diseases such as Alzheimer’s disease?
5. What secondary structure is most common in amyloid fiber formation?
6. What is a prion, and how does it act as an infectious agent.
7. A protein composed of 3 identical subunits is called a _____. A protein of 2 different subunits
is called a _____.
8. What are the advantages of quaternary structure?
9. Why does a larger protein move down a gel filtration column faster than a small protein?
10. What types of solid phases are used in ion exchange chromatography?
11. Use data from table 4.1 to estimate the pI of an Asp-Val dipeptide and a Lys-Cys dipeptide.
12. Why is the detergent SDS added to a protein mixture in gel electrophoresis?
13. Summarize five typical steps in the standard approach to sequencing a protein.
14. What information about a protein can be gathered from x-ray crystallography?