1- List and discuss the general strategies used by cells for the biological regulation of enzyme activity.
2- Define and provide an example of allosterism (both postitive and negative).
3- What are the similarities between hemoglobin and an allosteric enzyme?
10- Explain in structural terms the differences in substrate specificity of chymotrypsin, trypsin, and elastase.
11- Describe the general approaches that are used to determine the mechanism of catalysis of an enzyme. Include in the approaches how covalent modification, affinity labelling, inhibitor kinetics, structure deteminations, pH, site-directed mutagenesis, etc. facilitate the determination.
12- Describe the catalytic mechanism of chymotrypsin emphasizing the role the catalytic triad and substrate binding site play in catalysis.
Not covered in '98
4- Draw graphs illustrating homotropic and heterotropic regulation, using the enzyme ATCase as an example. Discuss the biological significance of this regulation.
5- Discuss the structural basis for allosterism in terms of R and T states.
6- Describe the structural changes which occur upon the activation of chymotrypsinogen.
7- Describe the structural changes which occur upon conversion of fibrinogen into fibrin during blood clot formation.
8- Describe the structural features of the active site of either lysozyme, chymotrypsin, or trypsin.
9- Describe the catalytic mechanism of lysozyme or chymotrypsin, emphasizing the role of protein functional groups in catalysis.