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Research School of Chemistry · ANU College of Science and Medicine
Many applications in modern chemistry and biochemistry depend on the ability to make, change and analyze proteins. After completion of the course, students will be familiar with all of the steps required for the production of proteins in bacteria, protein structural features and techniques for making, modifying (including the site-specific introduction of non-natural amino acids), and analysing proteins. There is an emphasis on biophysical techniques to characterise biomolecules (e.g., SDS-PAGE, light scattering, circular dichroism spectroscopy, ultracentrifugation, mass spectroscopy, surface plasmon resonance), including discussion of their physical basis. Advanced structural analysis techniques (X-ray crystallography, NMR spectroscopy, electron microscopy, solution scattering) are also discussed. An introduction to bioinformatics, i.e. protein sequence alignment, 3D structure analysis and modelling is also included. Note: This course is co-taught with undergraduate students but assessed separately.
Mid semester exam
Learning outcomes 1, 3, 4, 5
Laboratory and workshop based practicals (7 in total, 5% each).
Learning outcomes 2, 4, 5, 6
Final exam
Learning outcomes 1, 3, 4, 5
The expected workload will consist of approximately 130 hours throughout the semester including: - Face-to face component which may consist of 2 x 1 hour lectures and 1 x 1 tutorial per week; and 7 x 4 hour practicals across the semester. - Approximately 66 hours of self directed study which will include preparation for lectures, practicals and other assessment tasks. Other Information A pass in the prescribed laboratory work is required in order to gain a pass in this course.
Selected chapters from 'Biochemistry' by Voet & Voet, 4th edition Preliminary Reading Selected readings will be provided by individual lecturers