Exercise Questions

Q1. Explain the main conclusion of Griffith’s experiment.

Q2. There are 64 codons and 20 amino acids. Explain how these codons are used in encoding of amino
acids.

Q3. Explain what Chargaff’s rule is and how Erwin Chargaff came up with this rule?
Exercise Questions

Q1. What is central dogma? And explain each step.

Q2. What are the differences between DNA and RNA?

Q3. Define gene and allele.

Exercise Questions

Q1. What kinds of bonds hold the heavy chain fragment to the light chain fragment in the Fab?

Q2. Explain how ELISA works.

Q3. What are opsonization and agglutination? Which Ig have these two.

Q5. What is the main role of IgD?

Exercise Questions

Q1. Explain the difference between epimers and anomers. Give an example for each.

Q2. Why do cells need to store glucose in the form of glycogen and what is the structural advantage of
glycogen for animals as compared to either amylose or amylopectin?

Q3. What is the role of golgi apparatus for tagging of proteins.

Q4. What happens in cyclization process of glucose and why is the straight form of glucose more reactive
than the ring/cyclic form.
Exercise Questions

Q1. What is the difference between competitive and non-competitive inhibition? How do they affect the
Km and Vmax value of the target enzymes. You may draw a Lineweaver-Burk plot to show how these two
affect the Km and Vmax value of the target enzymes.

Q2. How can you find out that an enzyme is whether serine protease or not?

Q3. How do cells prefer to control the activity of enzymes in pathways?

Exercise Questions

Q1. Draw a typical Lineweaver-Burk plot and show what kind of information can be extracted from the
plot.

Q2. What are Vmax, Km, Kcat and enzyme efficiency?

Q3. For a given enzyme catalyzed reaction, the Michaelis constant is 0.2 mM and the substrate
concentration is 1.8 mM. What is the fractional saturation ([ES]/[ET]) of the enzyme under these
conditions?

Q4. A particular enzyme at a research facility is being studied by a group of graduate students. This enzyme
has a Km value of 5.0 X 10-6 M. The students study this enzyme with an initial substrate concentration of
0.055 M. At one minute, 7 µM of product was made. What is the amount of product produced after 5
minutes? What is the Vmax? (Hint: unit of velocity is µM/min)