1. Novel methods of the analytical and separation techniques in protein science. Structure analyses by mass spectrometry.
2. Selective modifications of amino acid side-chains in proteins.
3. Application of affinity and photaffinity labeling in studies of protein-ligand interactions.
4. Introduction of riporter groups. The significance of fluorescent and EPR probes in studies of protein conformation and dynamics.
5. Formation of cross bridges in proteins with the use of bifunctional chemical reagents. Immobilization of prorteins. Mapping of the structure of oligomeric and polimeric proteins.
6. Nonenzymatic protein modifications, in vivo.
7.Methods in proteomics.
8. Structure-function studies of proteins. The structural basis of enzyme action.
9. The structural basis of protein stability and flexibility.
10.The mechanism of action and design of proteases. The production of stable subtilisin and subtiligase by recombinant DNA techniques. The zymogen concept. Autolysis.
11. Function and mechanism of action of protease inhibitors. Assaying inhibitor action.
12. Design of protease inhibitors. Engineering of ecotin, blood-clotting factors and protease inhibitors from desert locust.
13. The mechanism of action of receptors. Beta-adrenerg, opiate and growth hormone receptors. Studying receptor-ligand interaction. Design and production of new ligands.
14. Pharmaceutical application of protein engineering: hormones, enzymes, inhibitors, monoclonal antibodies. The case of Genenentec, Inc., South San Francisco.
Some of the lectures are available at the website of Department of Biochemistry
Arthur Lesk: Introduction to Protein Science, OUP Oxford, 2010