Students

CBMS732 – Protein Discovery and Analysis

2014 – S1 Day

General Information

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Unit convenor and teaching staff Unit convenor and teaching staff Unit Convenor
Bridget Mabbutt
Contact via bridget.mabbutt@mq.edu.au
Credit points Credit points
4
Prerequisites Prerequisites
Admission to MRes
Corequisites Corequisites
Co-badged status Co-badged status
This Unit is co-taught with CBMS732 and CBMS832
Unit description Unit description
This unit outlines molecular principles underlying today's developments in protein science. As well as detailing modern separation technologies, the course addresses structural biology, protein analysis and sequence informatics. Practices common in the biotechnology and pharmaceutical industries to purify macromolecules (including recombinant proteins) are emphasized. Analysis methods are introduced in relation to proteomics, genomics and biomedical research. Molecular properties leading to the 3D shape of proteins are detailed, and contemporary structure methods outlined. Practical and project segments of the unit involve hands-on protein skills, molecular graphics and use of key protein web resources, and introduce opportunities for critical writing and interpretation.

Important Academic Dates

Information about important academic dates including deadlines for withdrawing from units are available at https://www.mq.edu.au/study/calendar-of-dates

Learning Outcomes

On successful completion of this unit, you will be able to:

  • Understand methods used today to isolate and handle proteins
  • Comprehend the molecular behaviour of proteins (gene products), both in vivo and in vitro
  • Develop a sound knowledge of protein structure and how it is encoded in a protein (or gene) sequence
  • Gain hands-on practical experience in protein characterisation, and competency with contemporary web tools
  • Exhibit a creative approach to articulating biomolecular forms and architectures
  • Extract, interpret and analyse information from a variety of scientific sources concerning proteins
  • Develop presentation skills (written, oral) relevant in biomedical science
  • Gain confidence in evaluating the scientific responses of peers

Assessment Tasks

Name Weighting Due
Final examination 40% University examination period
Laboratory reports 30% 28April, 5May, 26May
Pet Protein (Purification) 10% 7April
Pet Protein (Structure) 10% 3June or 10June
Pet Protein Model 10% 3June or 10June

Final examination

Due: University examination period
Weighting: 40%

This written exam will incorporate problem-solving exercises and 2 short essays. 


On successful completion you will be able to:
  • Understand methods used today to isolate and handle proteins
  • Comprehend the molecular behaviour of proteins (gene products), both in vivo and in vitro
  • Extract, interpret and analyse information from a variety of scientific sources concerning proteins

Laboratory reports

Due: 28April, 5May, 26May
Weighting: 30%

Laboratory reports must be submitted as a full report of your experimental data and discussion and analysis of your findings. Separate sections for Aims/Methods/Results & Discussion/References must all be included. 

Bibliography listings must conform to an acceptable style (for guidance, see www.mq.edu.au/on_campus/library/research/referencing/), or the report will be returned unmarked for correction and re-submission. 

In the case of the "Molecular Graphics" practical, your submitted report must fully conform to the style of the "Journal of Molecular Biology".

Laboratory reports must also be submitted in electronic form to the Turnitin program (see iLearn site for login details).  Marks will be deducted for reports handed in after the due date (5% / day).   

All written work (assignments and lab reports) are to be submitted via the assignment box located in the Science Centre (Room 101, Building E7A).    Submissions must include a completed and signed cover sheet stapled to the front cover.  Handwritten work will not be accepted. 

All marked work will be returned in class, generally within 3 weeks.

 


On successful completion you will be able to:
  • Understand methods used today to isolate and handle proteins
  • Comprehend the molecular behaviour of proteins (gene products), both in vivo and in vitro
  • Develop a sound knowledge of protein structure and how it is encoded in a protein (or gene) sequence
  • Gain hands-on practical experience in protein characterisation, and competency with contemporary web tools
  • Develop presentation skills (written, oral) relevant in biomedical science

Pet Protein (Purification)

Due: 7April
Weighting: 10%

This is a literature assignment and will require locating prime sources in books and journals. 

As your own case study, you will be allocated a protein of industrial/medical importance in class. You will undertake literature searches, conduct your own analysis utilising theory from lectures and construct interpretive flowcharts.



On successful completion you will be able to:
  • Understand methods used today to isolate and handle proteins
  • Comprehend the molecular behaviour of proteins (gene products), both in vivo and in vitro
  • Gain hands-on practical experience in protein characterisation, and competency with contemporary web tools
  • Extract, interpret and analyse information from a variety of scientific sources concerning proteins
  • Develop presentation skills (written, oral) relevant in biomedical science

Pet Protein (Structure)

Due: 3June or 10June
Weighting: 10%

Research the literature concerning the structure and structure determination methods relevant to your Pet Protein.

Transmit your understanding of the individual protein to your fellow students in seminar form.  You are required to :

- Describe the structural method(s) used to elucidate its structure.

- Outline the features and spatial organization of the molecule. 

- Describe structural features that relate to the function of your protein.



On successful completion you will be able to:
  • Develop a sound knowledge of protein structure and how it is encoded in a protein (or gene) sequence
  • Exhibit a creative approach to articulating biomolecular forms and architectures
  • Extract, interpret and analyse information from a variety of scientific sources concerning proteins
  • Develop presentation skills (written, oral) relevant in biomedical science

Pet Protein Model

Due: 3June or 10June
Weighting: 10%

Construct a model  (hint: wire, tape, kitchen utensils...) that shows the three-dimensional shape of your Pet Protein. You will be assessed on the extent to which your model successfully shows the shape and form of the protein in three-dimensions.

If your protein is particularly large, only one  domain need be demonstrated.


On successful completion you will be able to:
  • Develop a sound knowledge of protein structure and how it is encoded in a protein (or gene) sequence
  • Exhibit a creative approach to articulating biomolecular forms and architectures
  • Extract, interpret and analyse information from a variety of scientific sources concerning proteins
  • Gain confidence in evaluating the scientific responses of peers

Delivery and Resources

Your classes

 

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

Weekly tutorials (Friday 11 am or 12pm)will be used for additional material and problem solving-workshops. In the last weeks of semester, additional lectures may be delivered in this tutorial hour.

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. 

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.

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

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(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.

 

Weeks 1&2   -    
Week 3 18Mar

WORKSHOP: Searching the primary literature

 

 2-5pm, 832 and 732 students (E4B 118)

Week 4&5   -    
Week 6 7Apr   Pet Protein (Purification) due 832 and 732 students
  8Apr PRACTICAL: Mass spectrometry informatics   2-6pm, all students (E4B 118)

 mid-sem break

14-17Apr THREE-DAY PRACTICAL: Protein chromatography  

full days (E7B 349/350):

14,15,16Apr GRP A 15,16,17Apr Grp B

 Week 7 28Apr  - MassSpec report due  all students
 Week 8 5May   - Chromatography report due  all students
 Week 9 13May PRACTICAL: Molecular Graphics    2-6pm, all students (E4B 118)
 Week 10 20May  -    
 Week 11 26May    MolG report due  all students
  27May FILM: DNA-Life story    all students
 Week 12 3Jun SEMINARS: Pet Protein (Structure)   2-6pm, GRP A (venue tba)
 Week 13 10Jun SEMINARS: Pet Protein (Structure)   2-6pm, GRP B (venue tba)

 

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 (2nd 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:

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.

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.

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

Peer assessment task have been excluded this year to have a more balanced workload.

 

 

Unit Schedule

Lectures

1 - 3  

 

FUNCTIONAL GROUPS IN PROTEINS

 ISOLATING BIOMOLECULES

recombinant sources; quantitation & detection

5 & 6  

SEPARATION OF PROTEIN MIXTURES

separation  by precipitation; gel filtration for separation 

7 - 10   

CHROMATOGRAPHY FOR PURIFICATION

ion exchange; hydrophobic/reversed-phase; affinity chromatography

11 -13  

 PROTEIN ANALYSIS METHODS

 2D gel electrophoresis (MM);  mass spectrometry (PH); sugar/glycoprotein analysis (NP)

14 - 16

PROTEIN  FOLDS AND DOMAINS

all alpha-structures (globin fold, helix bundles); all beta structures (antiparallel barrels, the beta helix); mixed  alpha/beta folds

17- 19             

TERTIARY STRUCTURE DETERMINATION

 x-ray crystallography;  NMR spectroscopy

20 & 21

HOW PROTEINS FOLD IN SOLUTION

thermodynamics of protein folds; circular dichroism

22 & 23

BIOINFORMATICS

structure prediction methods;  the CASP project

24    

 MEMBRANE PROTEINS (KH)

25   FLUORESCENCE TECHNOLOGIES (LB)

 

      

    

Policies and Procedures

Macquarie University policies and procedures are accessible from Policy Central. Students should be aware of the following policies in particular with regard to Learning and Teaching:

Academic Honesty Policy http://mq.edu.au/policy/docs/academic_honesty/policy.html

Assessment Policy  http://mq.edu.au/policy/docs/assessment/policy.html

Grading Policy http://mq.edu.au/policy/docs/grading/policy.html

Grade Appeal Policy http://mq.edu.au/policy/docs/gradeappeal/policy.html

Grievance Management Policy http://mq.edu.au/policy/docs/grievance_management/policy.html

Disruption to Studies Policy http://www.mq.edu.au/policy/docs/disruption_studies/policy.html The Disruption to Studies Policy is effective from March 3 2014 and replaces the Special Consideration Policy.

In addition, a number of other policies can be found in the Learning and Teaching Category of Policy Central.

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Macquarie University students have a responsibility to be familiar with the Student Code of Conduct: https://students.mq.edu.au/support/student_conduct/

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Macquarie University provides a range of support services for students. For details, visit http://students.mq.edu.au/support/

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Students with a disability are encouraged to contact the Disability Service who can provide appropriate help with any issues that arise during their studies.

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