CHEM 4630
Biochemistry of Proteins
CHEM 4630 Biochemistry of Proteins (3)
(Formerly 002.463) The structure and function of proteins, their physical and chemical properties and methods for studying them. Not to be held with CHEM 4631. Prerequisite: a "C" or better in one of CHEM 2370, CHEM 2371 (002.237), MBIO 2370, MBIO 2371 (060.237), the former 002.235, or the former 060.235.
Announcements
Please read this important notice from the
Faculty of Science:
Registration Advisory.
Note also that Tuesday January 17 is the last day for adding courses and
VW day is Friday March 16.
Course Outline - 2012
Lectures:
- TR 11:30 AM – 12:45 PM
- 111 Armes Building
Instructor:
Joe O'Neil
Office:
Textbook:
none required
References:
- File of papers that can be borrowed from me.
- Proteins: Structures and Molecular
Properties
by Thomas E. Creighton (1st or
2nd edition)
W.H. Freeman & Co. 1984, 1989
QP551.C737
- Introduction to Protein Structure
by C. Branden & J. Tooze
1st or 2nd edition
Garland Publishing, Inc. 1991
QP551.B7635
(available in bookstore).
- Biophysical Chemistry Part 2
by C.R. Cantor and & P.R. Schimmel
Freeman & Co.
QH345.C36.
- Structure in Protein Chemistry
by Jack Kyte
Garland Publishing, Inc. 1995
QP551.K98 (available in bookstore).
- Copies of midterm and final examinations from previous years are
are available on-line at:
Online Examinations, and are listed below.
Working through them will help prepare you for the examinations.
Evaluation:
| Mid-Term Test 1 (in-class) Thursday February 9 |
20% |
Essay due Tuesday February 28 |
20% |
Mid-Term Test 2 (in-class) Tuesday March 20 |
20% |
Final Exam set by Student Records (3 hr.) |
40% |
Note:
- VW day is Friday, March 16.
Final Exam Review
Students in the Faculty of Science are permitted to review their final exams before the deadline for appealing final grades (Final Grade Appeal). If you wish to view your final exam please go to the Department of Chemistry general office (360 Parker Building), fill in an application form, and pay the $5.00 fee. You can also fill in the form that can be found on the Department of Chemistry www site at Undergraduate Program under "Links & Forms".
Academic Dishonesty: Please visit
the Faculty of Science web site
Cheating, Plagiarism etc.
Topics:
- Protein Primary Structure
- HPLC Chromatography, Capillary
Electrophoresis, Immobilized Metal Chelate Chromatography
- Amino Acid Analysis, Protein Sequencing
- Hydrodynamics
- Mass Spectrometry and Proteomics
- Peptide Synthesis
- Applications of Peptide Methods, Circular Dichroism, Fluorescence
- Protein Secondary and Tertiary
Structure
- α-helix,
β-sheet,
turns, and others
- Motifs and Domains
- All α
Proteins, All β
Proteins, Green Fluorescent Protein, α+β
Proteins
- Membrane Proteins
- Protein dynamics
- Protein folding in cells
- The Protein Folding Problem
Essay Guideline:
- Select a research paper dealing with protein structure or
function from a journal published
in 2011/12. Note: This paper must be approved by
me before you begin writing your essay. Review articles
are not acceptable. Suggested journals include Biochemistry,
Journal of Biological Chemistry, Nature, Science, PNAS, Proteins:
Structure, Function and Genetics, Protein Science but not
Scientific American. In your essay describe and explain
the research presented in the paper. Begin with a background
section (Introduction) in which you familiarize your readers (e.g.
4th year students) with the scientific problem tackled by the
authors. Use references as appropriate but note that the purpose
of the paper is not to do an exhaustive literature search. Explain
the methods used by the authors to solve the problem and explain
the interpretations of the data presented. Are other interpretations
possible? Finally, describe questions that are still unanswered
when the results of the paper are considered. Suggest experiments
that might answer those questions but note that the paper is
not to be a research proposal. Make sure you give credit
to all sources of information in the text of your essay
not just at the end. In this exercise, direct quotes from other authors are generally inappropriate as your task is to explain the concepts in your own words.
- The essay should be approximately 2,500
words in length, preferably typed double spaced. Neat handwriting
is acceptable. Note that grammar and spelling will be worth
15% of the essay mark. Use Figures to explain difficult or complicated
concepts. Please provide 1 photocopy of the research
paper with your essay. It is also a good idea to keep a copy of your essay for yourself.
- The penalty for late essays is 5%/week;
the first penalty is applied 7 days after the deadline. Essays
cannot be accepted after the end of classes.
- Essay Marking Guideline
- *** This is under construction ***Please fill out the essay submission form here: Testform
Protein Dynamics Movies:
The following two movies were taken from the WWW site
(Dr. Kneller's WWW Site)
of Prof. Dr. G. Kneller, Centre de Biophysique Moleculaire, F-45071 Orleans. The first movie
shows the motions of the 8 alpha-helices of Myoglobin during a 24 picosecond dynamics simulation:
Myoglobin Helices
The next movie shows the liquid-like dynamics of some of the side-chains in the protein
over the same period of time. These are the motions that permit oxygen to diffuse from the
external environment into the protein interior where it binds to the heme iron.
Myoglobin Side-Chains
The next movie was taken from the WWW site ( Dr. Onufriev's WWW site
) of Dr. Alexey Onufriev of the Departments of Computer Science and P
hysics at Virginia Tech.
It
shows Myoglobin in a space-filling representation. In the interior are cavities big enough to hold an oxygen molecule. Over 15 ps, movements of side-chains changes the positions of the cavities permitting oxygen
to diffuse through the protein to the heme. According to Dr. Onufriev, there is only
one pathway that will permit oxygen to diffuse from outside the protein to the heme.
Myoglobin Cavity Dynamics
The next movies were taken from the WWW site (Dr. Gerstein's WWW Site
) of Dr. Mark Gerstein of Yale University Departments of Molecular Biophysics and Biochemistry
and Computer Science. They illustrates several views of the large conformational change that the Chaperonin
large sub-unit GroEL underogoes between the open and closed states of the Anfinsen cage.
GroEL Spacefilling Representation
GroEL Ribbon Representation
GroEL Rotated
Useful Web Sites for CHEM 4630:
PDB WWW Server
SCOP: Structural Classification of Proteins
Database of Macromolecular Movements
Return to the Chemistry Department Course Descriptions
Return to Joe O'Neil's Home Page
http://home.cc.umanitoba.ca/~joneil/CHEM4630.Course.outline.htm
Maintained by J. O'Neil
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