Learning Outcomes:
On completion of this module students should be able to: 1. Understand how NMR, X-ray crystallography and electron microscopy can be used to determine biological strucures. 2. Utilise a range of biological techniques for examining protein-protein, protein-ligand and protein-DNA interactions. 3. Acquire a detailed understanding of how antibody-antigen, receptor-ligand and protein-protein interactions and can be applied to combat disease. 4. Understand how data on protein-DNA interactions are applied to understand biological functions at the genome level. 5. Understand the post translational processing of proteins and protein trafficking. 3. Determine catalytic constants kcat, KM, kcat/KM and the values of the inhibition constants Ki and IC50. 6. Measure pKa values in free enzymes and enzyme-substrate complexes. 7. Understand how enzymes can utilise transition state stabilisation, ground state stabilisation, nucleophilic, catalysis, electophilic catalysis, general acid-base calysis and binding/entropic catalysis to catalyse reactions. 8. Be aware of some of the ways ribozymes and catalytic antibodies can be used in medicine. 9. Utilise site directed mutagenesis to identify essential amino acids. 10. Protein design and industrial applications of mutagenesis experiments.