Five modes of assessment are used to determine your progress in CBMS332. Satisfactory (i.e pass level) performance must separately be achieved in all four of the assessment areas to pass this Unit.

Your Classes

• Lectures will be twice weekly: Thursday (9 am) in E6A 102 theatrette and Thursday (1 pm) in W5C 320.  
• It is essential that you be available to attend all the classes in person.  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 lecture through illness or misadventure, please contact Dr Shah in iLearn to organise access to the relevant lecture file.
• iLectures will be released for revision purposes from teaching week 12.
• The course syllabus is defined by the subject material presented in all  lectures (including guest lectures) and practicals, much of which is beyond standard textbooks.
• From week 2, tutorials run for all students twice a week. These are structured as problem-solving workshops. You are required to attend for either of the two days. An additional lecture may be delivered in these tutorial hours.

Laboratory Sessions

• A block practical is scheduled in the first week of mid-semester break, i.e. from April 11 – 15.  You will be allocated a lab group by the Unit convenor and be required to attend for either Mon-Wed (Apr 11-13) or Wed-Fri (Apr 13-15) of the practical week.
• During session, workshops (named Practical_1 in the University timetable) are scheduled on several Thursday afternoons (2-6 pm).  You will attend for 3 afternoons, according to your allocated laboratory group.
• Attendance is compulsory on the allocated days of class. If you are sick, please consult with the Unit Convenor to ensure all laboratory and project work is completed.  Outstanding reports 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 expected to purchase 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.  The library has an excellent collection of up-to-date reference material to cover the course and laboratory subjects - explore it!!

• 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, 2009
  • “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, 2013
  • 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.

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. 

Lectures

1 - 3           FUNCTIONAL GROUPS IN PROTEINS

4                ISOLATING BIOMOLECULES

5 & 6          SEPARATION OF PROTEINS

7 & 8          PROTEIN ANALYSIS

9                FLUORESCENCE TECHNOLOGIES (LB)

10 - 13       CHROMATOGRAPHY FOR PURIFICATION

14              PROTEIN ANALYSIS (cont.)

15 - 17       PROTEIN  FOLDS AND DOMAINS

18 - 20       TERTIARY STRUCTURE DETERMINATION

21 & 22      HOW PROTEINS FOLD IN SOLUTION

23 & 24      BIOINFORMATICS

25              MEMBRANE PROTEINS