Biochemistry BCEM
Instruction offered by members of the Department of Biological Sciences in the Faculty of Science and Department of Biochemistry and Molecular Biology in the Faculty of Medicine.
Department Heads - D.M. Reid (Biological Sciences), L.W. Browder (Biochemistry and Molecular Biology)
Students interested in taking Biochemistry courses are urged to read the advice in the Faculty of Science Program section of this Calendar.
"DAGGER" Limited amounts of non-scheduled class time involvement will be required for these courses.
Senior Courses
Biochemistry 341 H(3-3/2)
Biochemistry of Life Processes
Emphasis is placed on describing the chemistry of biochemical molecules including proteins, carbohydrates, lipids, and nucleic acids, and how this relates to cell structure. The metabolism of carbohydrates and lipids.
Prerequisites: Chemistry 341 or 351.
Note: Credit for both Biochemistry 341 and either 393 or 443 will not be allowed.
Note: Not open to majors in the Department of Biological Sciences or Natural Sciences concentrators in Biological Sciences.
Biochemistry 393 H(3-3/2)
Introduction to Biochemistry
The structure and function of carbohydrates, amino acids, proteins, lipids, coenzymes and enzymes will be presented, along with an introduction to metabolism and energy transduction. Laboratory: Modern biochemical techniques for analysis of carbohydrates, amino acids, lipids, proteins, enzymes and metabolism.
Prerequisites: Biology 311 and Chemistry 351.
Corequisites: Biology 331.
Note: Credit for both Biochemistry 393 and 341 will not be allowed.
Biochemistry 401 H(3-6)
Biochemistry Laboratory Techniques I
Laboratory safety, centrifugation, data analysis, use of radioisotopes, methods of protein expression and characterization. Practical experience in the laboratory with protein expression, bioinformatics and a selection of protein characterization techniques.
Prerequisites: One of Chemistry 353 or 355; and Biochemistry 393.
Corequisites: Prerequisites or Corequisites: Chemistry 311, 315 and Biochemistry 471.
Note: Credit for both Biochemistry 401 and 541 will not be allowed.
Note: Enrollment in this course may be limited. See explanation in Program section of Calendar.
Biochemistry 403 H(3-6)
Biochemistry Laboratory Techniques II
Chromatography, protein purification, biophysical and enzymatic means of characterizing proteins. Practical experience in the laboratory with protein purification and protein characterization techniques selected to complement the selection from Biochemistry Laboratory Techniques I.
Prerequisites: One of Chemistry 353 or 355; and Biochemistry 393.
Corequisites: Prerequisites or Corequisites: Chemistry 311, 315 and Biochemistry 471.
Note: Credit for both Biochemistry 403 and 541 will not be allowed.
Note: Enrollment in this course may be limited. See explanation in Program section of Calendar.
Biochemistry 431 H(3-0)
(formerly Biochemistry 531)
Proteins and Proteomics
Protein structure and chemistry: structural motifs, ligand-binding, conformational changes, chemical modification; protein folding; structure prediction by molecular modeling. Identification of proteins in the proteome: 2D gel electrophoresis and chromatography, mass spectrometry; metalloproteins; post-translational modifications; protein-protein interactions.
Prerequisites: Biochemistry 393.
Biochemistry 443 H(3-4/2)
Metabolism and the Synthesis of RNA, DNA and Protein
Enzyme mechanisms and regulation, intermediary metabolism and its regulation, nucleic acid biochemistry, structure and stability, and the synthesis of nucleotides, DNA, RNA and proteins. The laboratory experiments will include enzymology, metabolic studies, nucleic acid chemistry and protein expression.
Prerequisites: One of Chemistry 353 or 355; and Biochemistry 393.
Note: Credit for both Biochemistry 443 and 341 will not be allowed.
Note: Enrollment in this course may be limited. See explanation in Program section of Calendar.
Note: Not required for majors in the Biochemistry program.
Biochemistry 471 H(3-2T)
Physical Biochemistry
The laws of thermodynamics as they apply to biological systems: the hydrophobic effect, properties of water, electrolyte solutions and ligand binding. Optical spectroscopic methods including UV/visible absorption, fluorescence, circular dichroism, and infrared as applied to biological molecules.
Prerequisites: Biochemistry 341 or 393; Chemistry 341 or 353 or 355; one of Mathematics 249, 251 or 261 and one of Mathematics 253, 263, 211 or 221; one of Physics 211 or 221, and 223.
Biochemistry 507 H(3-3)
Special Problems in Biochemistry
Lectures, seminars, term papers and training in theoretical and/or laboratory methods. After consultation with a Departmental faculty member who will supervise the chosen problem, a permission form obtained from the Department Office must be signed by the course supervisor before a student can register.
Prerequisites: Third or higher-year standing and consent of the Department.
MAY BE REPEATED FOR CREDIT
Biochemistry 528 F(0-6)
Independent Studies in Biochemistry
Original and independent thought, practical research and the completion of written and oral reports. After consultation with a Departmental faculty member who will supervise the chosen problem, a permission form obtained from the Department Office must be signed by the course supervisor before a student can register.
Prerequisites: Fourth-year standing and consent of the Department.
MAY BE REPEATED FOR CREDIT
Biochemistry 530 F(0-8)
Honours Research Project in Biochemistry
Research project under the direction of one or more faculty members in the Department of Biological Sciences. Formal written and oral reports must be presented on completion of this course. Open only to Honours Biochemistry students or Honours Biological Sciences students. After consultation with a Department faculty member who will supervise the chosen problem, a permission form obtained from the Department Office must be completed before a student can register.
Prerequisites: Fourth-year standing and consent of the Department.
Note: Active participation in Divisional seminar programs is a requirement of this course.
Biochemistry 537 H(3-0)
(Medical Science 537)
Nucleic Acids
Chemical structure and physical characterization of nucleic acids. DNA topology. DNA transcription and repair. Nucleic acid-protein interaction as related to transcription and chromosome structure. Cloning of DNA and analysis of recombinant molecules. Recombinant DNA molecules and cloning of DNA.
Prerequisites: Biochemistry 443.
Biochemistry 543 H (3-0)
Enzymology
The structure, mechanisms and biological interactions of enzymes. Binding, catalysis, rates and regulation will be discussed with regard to chemical principles of kinetics and reaction. The principles of enzyme action will be considered in the context of the biological role that enzymes play.
Prerequisites: Biochemistry 393 and Chemistry 353 or 355.
Biochemistry 547 H(3-0)
Regulation of Metabolism and Signal Transduction
The structure, function, compartmentation of selected metabolic pathways in microbes, plants and animals: carbohydrate metabolism, lipid and steroid biosynthesis and nitrogen metabolism, signal transduction pathways from the membrane to the nucleus and structure and function of protein kinases and protein phosphatases.
Prerequisites: Biochemistry 443.
Biochemistry 551 H(3-0)
Structural Biology
Applications of modern methods to structural studies of proteins and nucleic acids by NMR and X-ray crystallography with a comparison of the structural information derived from the two methods. Crystallization of macromolecules. Experimental and theoretical foundations of X-ray and NMR structure determination, and ligand binding. Non-invasive NMR studies of metabolism, and magnetic resonance imaging.
Prerequisites: Biochemistry 471.
Biochemistry 555 H(3-0)
Biomembranes
The structure and function of biological membranes with emphasis on membrane proteins. Topics will include the properties of lipid bilayers, isolation and purification of membranes, preparation of model membrane systems, energetics of membrane potentials and transport, membrane protein function, folding, assembly and structure, and protein secretion and targeting.
Prerequisites: Biochemistry 443.
Corequisites: Prerequisite or Corequisite: Biochemistry 471.
Biochemistry 561 H(2-3T)
(formerly Biotechnology 561)
Applied Biochemistry and Biotechnology
An introduction to the language, materials, methods, concepts and commercial applications of biotechnology with emphasis on methodology: biocatalysts, bioreactor designs and operation, scale-up, instrumentation, product recovery, animal and plant cell culture, process economics.
Prerequisites: Biochemistry 443 and Biology 311.
Biochemistry 577 H(3-4/2)
Biomolecular Simulation
Introduction to simulation and computer modelling methods commonly used in biochemistry and biophysics, with a focus on physical models to understand the behaviour of biomolecules. Topics include simulation methods, dynamics of proteins, DNA, and lipids, calculation of binding constants, protein-drug interactions, properties of ion channels as well as a number of recent literature topics.
Prerequisites: One of Biochemistry 341 or 393 and Biochemistry 471 or Chemistry 371.
Graduate Courses
Enrollment in any graduate course requires consent of the Department.
Only where appropriate to a student's program may graduate credit be received for courses numbered 500-599.
600-level courses are available with permission to undergraduate students in the final year of their programs.
See also the separate listing of graduate level Chemistry courses.
Biochemistry 641 H(3-0)
Selected Topics in Biochemistry
Selected topics in Biochemistry such as those which appear annually in the serial publication Annual Review of Biochemistry.
MAY BE REPEATED FOR CREDIT
Biochemistry 731 H(3-0)
Protein and Metabolic Engineering
Contemporary methods of recombinant DNA technology will be combined with modern methods and strategies for expressing, secreting, purifying and characterizing engineered proteins and enzymes. Genetic engineering of metabolic pathway design and regulation will also be dealt with. The emphasis will be on the utilization of these techniques as tools for studying proteins and metabolism.