1. Describe how the cooperative binding of oxygen by hemoglobin makes it a better oxygen transporter.

2. Define the "R" (relaxed) and "T" (tense) states of hemoglobin.

3. Describe the relationship of the Bohr effect to oxygen binding by hemoglobin and explain the physiological significance of this effect.

5. Explain the effect of 2,3-bisphosphoglycerate (BPG) on hemoglobin affinity for oxygen and how it facilitates oxygen release to tissues.

6. Explain why the low affinity of fetal hemoglobin for BPG is beneficial to the fetus.

1. Diagram the basic structure common to immunoglobulins.

2. Define the following terms related to immunoglobulin structure: heavy chain, light chain, constant region, variable region, hinge region, Fab fragment, Fc fragment and complementarity-determining regions (CDRs).

3. Describe the different forces involved in the binding of an antibody to its antigen and define the term hapten.

1. Describe the following terms associated with enzymes: catalysis, substrate, reaction specificity, rate-limiting step, coenzyme and prosthetic group.

2. Define the following six types of enzyme reactions: transferase, hydrolase, oxidoreductase, lyase, ligase and isomerase.

3. Define the following terms related to the energy of enzyme reactions: transition state, energy of activation, exergonic, endergonic and free energy change.

4. Discuss the concepts of substrate affinity, K_m and apparent K_m.

5. Use the Lineweaver-Burke plot to demonstrate V_max, K_m, competitive inhibition and non-competitive inhibition.

Define the structure of lactose and discuss how a lactase deficiency can provoke physiological symptoms.