Your classes

Lectures will be twice weekly: Tuesday (9 am) and Wednesday (10 am).  

It is essential that you be available to attend all lectures.  ilectures are NOT made available during session, as the classroom experience is integral to the subject material of this Unit. 

Should you miss a specific class (illness or misadventure), please contact the Unit Convernor in iLearn  to organise access to the relevant iLecture file.

The course syllabus is defined by all of the subject material presented in lectures (including guest lectures) and practicals, much of which is beyond standard textbooks.

Weekly tutorials for problem-solving exercises aimed at the post-graduate group of students (Friday 11 am or 12pm), will be optionally open to the CBMS332 group. In the last weeks of semester, additional lectures may be delivered in this Tutorial hour.

Laboratory Sessions:

A 3-day block practical on Protein chromatography is scheduled in the mid-semester break (first week).

During session, additional practical tasks are scheduled on Tuesday afternoons (2-6 pm).  You will attend  ~5 afternoons according to your allocated laboratory group.  

Attendance is compulsory on all allocated days of class. If you are sick, please consult the Unit Convenor in iLearn to ensure all laboratory and project work is completed.  Outstanding practical work will result in failure of this Unit.

Please carefully check the location of each laboratory activity, as classes start promptly.  Latecomers may be excluded from class.

Required and recommended texts

The textbook of which you are required to obtain a personal copy is:  “Physical Biochemistry: Principles and Applications”, David Sheehan, John Wiley (2^nd ed, 2002).

Because of the multidisciplinary nature of this course, you will be expected to read more widely than this, however.   

Strongly recommended reference texts available in the library (short-term loan only):

“Proteins: Structure and Function”, D. Whitford, John Wiley, 2005

“Protein Structure and Function”, Petsko & Ringe, New Science Press, 2004

“Introduction to Protein Structure”, Branden & Tooze, Garland, 1999

“Purifying proteins for proteomics : a laboratory manual” ed. R.J. Simpson. Cold Spring Harbor Laboratory Press, 2004

Other general references that you may find useful are:

R. Scopes, "Protein purification: principles and practice", New York, Springer-Verlag, 1994

Garrett & Grisham, “Biochemistry” (esp. Chs 4 – 6), Harcourt Brace, 1999

T. Creighton, “Proteins: Structures and Molecular Properties”, Freeman, 1993

Web resources

The Unit will run as an online unit within iLearn (http://learn.mq.edu.au).  Within this Unit, you will be introduced to Web-based tools, search engines and graphics software that are commonly used today in protein science. There are many excellent websites, apps and YouTube presentations to show how protein are made and constantly move around. 

It is an expectation that you will become familiar with the following sites during the course:

• www.uniprot.org/

This is a centralised resource for “vital statistics” of known proteins.  Try out your Pet Protein here!

• http://au.expasy.org

“Proteomics” website hosted by the Swiss Intitute for Bioinformatics.  Provides many of the tools for doing your own protein analysis & bioinformatics.  Good links, so start here.

• www.ncbi.nlm.nih.gov/pubmed (or just type Pubmed)     

Essential for your literature searches-free and easy searching of all journals- anywhere, anytime.

• www.rcsb.org/pdb        (or just type PDB)

the world’s  central protein structure database. Use this to locate structures and view them in 3D.

• www.sunsetlakesoftware.com (or AppleStore)

free downloadable  “Molecules” application:

“an application for the iPhone and iPod touch that allows you to view three-dimensional renderings of molecules and manipulate them using your fingers. You can rotate the molecules by moving your finger across the display, zoom in or out by using two-finger pinch gestures, or pan the molecule by moving two fingers across the screen at once.”

Technology Requirements

Within this Unit, you will be introduced to Web-based tools, search engines and graphics software that are commonly used today in biomedical science. You will require internet access and a computer for web browsing, preparation of your reports and case study analysis.  Your project and laboratory reports will be submitted and circulated via the online Turnitin program.

Your practical reports will require you to carry out minor computational tasks, for which a calculator and access to basic statistical software will be required. We place a large emphasis on correct referencing style in all your reports, and use of the program EndNote is encouraged, but not essential.

The capacity to download and install a simple molecular graphics program will assist you greatly in the Unit. Your model-building assessment task can be carried out with very simple materials; it is not an expectation that expensive art supplies need be purchased. 

New for 2014

Methods of protein isolation and characterisation will be tested by a mid-semester test rather than a research report.  This exam will test material covered within lectures 1-10.

Molecular graphics practical will report as a reflective essay, not a formal practical report.