BMC3081

Spectroscopy ( 6 points, SCA Band 2, 0.125 EFTSL)

Leader: Dr Martin Scanlon

Offered:
Parkville First semester 2006 (Day)

Synopsis: Advanced spectroscopy develops concepts that were introduced in the second year subject Introduction to Spectroscopy and examines the relationship between the chemical structure of a molecule and its physical and spectroscopic properties. The use of spectroscopic and spectrometric methods in the analysis of molecules and in the measurement of intermolecular interactions will be described.

Objectives: At the completion of this unit the participant will be able to: 1. Analyse and interpret two dimensional spectra so as to identify the chemical structures of compounds 2. Define the term nuclear Overhauser enhancement (NOE) and account for the observation of NOEs in one-dimensional and two-dimensional NMR spectra of both small and large molecules 3. Analyse and interpret NOE data to determine the conformation of small molecules 4. Analyse and assign two-dimensional NMR spectra of small peptides 5. Describe quantitatively the relationship between enthalpy, entropy and free energy 6. Describe quantitatively the relationship between changes in free energy and equilibrium 7. Apply the concepts of this thermodynamics module to selected examples of biochemical energetics, protein-drug binding and drug-receptor interactions 8. Describe the principal NMR-based strategies for drug discovery and design 9. Use mass spectral data for structural elucidation. 10. Understand how to select an appropriate ion source method for a mass spectral study of a compound. 11. Understand and select among the various methods for mass analysis, and the use of collision-induced dissociation (CID) to solve structural problems involving biomolecules. 12. Describe the use of GC-MS and LC-MS for the study of pharmaceuticals and drugs. 13. Analyze mass spectral fragmentation patterns for important compound classes including carbohydrates, lipids, amino acids, peptides, and proteins. 14. Use and interpret mass spectral data for proteomics. 15. Describe how circular dichroism spectroscopy is useful for elucidation of secondary structure in proteins and nucleic acids. 16. Describe sampling methods and instrumentation available for IR and Raman spectroscopy and select the most suitable techniques for various applications on an informed basis 17. Detail the factors which govern photon-initiated electronic excitation, and describe the processes by which molecules can relax. In particular, to describe the phenomena and applications associated with fluorescence 18. Apply their knowledge of quantum theory and photophysical processes to interpret electronic and vibrational spectra 19. Measure and record data relevant to the understanding of drug structure and reactivity 20. Perform numerical calculations based on experimental or theoretical data 21. Present written or oral results of experimental work.

Assessment: End of semester exam: 60% (3 hours), Mid-semester exam: 20%, Practical work: 20%

Corequisites: The other core compulsory subjects of the Bachelor of Medicinal Chemistry.