CHEM3204 Structural biology
Later Year Course
| Offered By | Research School of Chemistry |
|---|---|
| Academic Career | Undergraduate |
| Course Subject | Chemistry |
| Offered in | First Semester, 2013 and First Semester, 2014 |
| Unit Value | 6 units |
| Course Description |
Modern chemistry and biochemistry depends on the ability to make, change and analyse proteins and enzymes. This course focuses on the three-dimensional structures of proteins. It includes (I) the prediction of 3D structures by bioinformatic tools, (II) their analysis by X-ray crystallography, NMR spectroscopy and other techniques (e.g. chemical cross-linking and mass-spectrometry), (III) protein design, (IV) protein dynamics and folding and (V) structure-based drug discovery. The physical basis of the techniques will be discussed in depth. Wherever possible quantitative examples will be given – students will be expected to solve numerical problems. After completion of the course students will be able to view 3D structures of proteins, deduce properties from their structures and make structure-function predictions for mutants. The practicals associated with the course practice all of the steps required for the production of mutant proteins in E. coli in vivo and provide hands-on experience with bioinformatics tools and spectroscopic techniques of analysis. |
| Learning Outcomes |
On satisfying the requirements of this course, students will have the knowledge and skills to: 1) Capability to make mutant gene constructs, (LO-1) 2) Capability to express proteins in vivo, (LO2) 3) Capability to purify proteins from E. coli, (LO3) 4) Ability to analyse proteins with spectroscopic analysis. (LO4) 5) Detailed understanding of X-ray crystallography and NMR spectroscopy for 3D structure determination of proteins, (LO5) 6) Understanding of structure-activity and dynamics-activity relationships of proteins, (LO6) 7) Ability to use bioinformatics tools for the prediction of protein properties. (LO7) 8) Capability to solve numerical problems associated with each course component. (LO8) |
| Indicative Assessment |
50% by written exam, (LO 4,5,6 & 8) 50% by weekly assessments of practicals and tutorials (10 in total, 5% each). (LO 1- LO8) |
| Workload |
65 hours of lectures/tutorials/laboratory plus a further 65 hours of independent learning. |
| Areas of Interest | Chemistry |
| Requisite Statement |
Prerequisite: CHEM2208 |
| Incompatibility |
Incompatibility: CHEM3041 |
| Recommended Courses |
Required skills: essential laboratory skills (pipetting, weighing, pH measurement) |
| Prescribed Texts |
Recommended: Voet & Voet, Biochemistry (4th Ed.). How Proteins Work. M.P. Williamson. |
| Majors/Specialisations | Chemistry |
| Science Group | C |
| Academic Contact | Professor Gottfried Otting |
The information published on the Study at ANU 2013 website applies to the 2013 academic year only. All information provided on this website replaces the information contained in the Study at ANU 2012 website.
