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.
Upon successful completion, students will have the knowledge and skills to:
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)
Other InformationYou will need to contact the Research School of Chemistry at firstname.lastname@example.org to request a permission code to enrol in this course.
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)
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65 hours of lectures/tutorials/laboratory plus a further 65 hours of independent learning.
This course is taught in intensive mode. Classes run from 27 June to 8 July 2016. The final examination is expected to be held on Friday 22 July 2016.
Requisite and Incompatibility
Recommended: Voet & Voet, Biochemistry (4th Ed.). How Proteins Work. M.P. Williamson.
Tuition fees are for the academic year indicated at the top of the page.
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- Student Contribution Band:
- Unit value:
- 6 units
If you are an undergraduate student and have been offered a Commonwealth supported place, your fees are set by the Australian Government for each course. At ANU 1 EFTSL is 48 units (normally 8 x 6-unit courses). You can find your student contribution amount for each course at Fees. Where there is a unit range displayed for this course, not all unit options below may be available.
Offerings, Dates and Class Summary Links
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Class summaries, if available, can be accessed by clicking on the View link for the relevant class number.
|Class number||Class start date||Last day to enrol||Census date||Class end date||Mode Of Delivery||Class Summary|
|6622||27 Jun 2016||04 Jul 2016||22 Jul 2016||22 Jul 2016||In Person||N/A|