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 - J.I. Goldberg (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.
鈥燣imited amounts of non-scheduled class time involvement will be required for these courses.
Senior Courses
Biochemistry 341
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. Course Hours:H(3-3/2) Prerequisite(s):Chemistry 351. Antirequisite(s):Note: Credit for both Biochemistry 341and393 will not be allowed. Notes: Not open to majors in the Department of Biological Sciences or Natural Sciences concentrators in Biological Sciences.
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. Course Hours:H(3-3/2) Prerequisite(s):Biology 311or Medical Sciences 341 (BHSc students only), and Chemistry 351. Antirequisite(s):Note: Credit for both Biochemistry 393and341 will not be allowed. Notes: Prior or concurrent completion of Biology 331 is strongly recommended.聽 Biochemistry 393and443 are the recommended courses for students wishing to take only two biochemistry courses. These courses cover biochemistry broadly and include the topics students are expected to understand prior to admission to Medicine, Veterinary Medicine, Dentistry, Optometry and other professional schools having two courses in biochemistry as recommended preparation or requirements for admission.
Recombinant DNA techniques, protein expression and mutagenesis stressing nucleic acid and protein properties relevant to these techniques. Practical experience in the laboratory includes DNA amplification (PCR), gene cloning and expression, nucleic acid-protein bioinformatics and introduction to methods for working with proteins. Emphasis on the scientific process: experimental design, data analysis and dissemination of results. Course Hours:H(3-6) Prerequisite(s): One of Chemistry 353or355; and Biochemistry 393. Antirequisite(s):Note: Credit for both Biochemistry 401andeither 541orCellular, Molecular and Microbial Biology 451 will not be allowed. Notes: Enrolment in this course may be limited. See Enrolment Limitations in Courses in the Faculty of Science section of this Calendar.
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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. Course Hours:H(3-6) Prerequisite(s):Chemistry 311andBiochemistry 393and471. Antirequisite(s):Note: Credit for both Biochemistry 403and 541 will not be allowed. Notes: Enrolment in this course may be limited. See Enrolment Limitations in Courses in the Faculty of Science section of this Calendar.
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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. Course Hours:H(3-0) Prerequisite(s):Biochemistry 393andoneofChemistry 353or355. Also known as:(formerly Biochemistry 531)
Intermediary carbohydrate, lipid and nitrogen metabolism, and the regulation of these metabolic pathways; nucleic acid chemistry, structure, stability and enzymatic processing. Course Hours:H(3-4/2) Prerequisite(s): One of Chemistry 353or355; and Biochemistry 341or393. Notes: Enrolment in this course may be limited. See Enrolment Limitations in Courses in the Faculty of Science section of this Calendar. Not required for majors in the Biochemistry 辫谤辞驳谤补尘.听 Biochemistry 393and443 are the recommended courses for students wishing to take only two biochemistry courses. These courses cover biochemistry broadly and include the topics students are expected to understand prior to admission to Medicine, Veterinary Medicine, Dentistry, Optometry and other professional schools having two courses in biochemistry as recommended preparation or requirements for admission.
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. Course Hours:H(3-2T) Prerequisite(s):Biochemistry 341or393; Chemistry 353or355; one of Mathematics 249, 251, 261or281andoneofMathematics 253, 263, 283, 211, 213or 221; one of Physics 211or221, and223.
Lectures, seminars, term papers and training in theoretical and/or laboratory methods. Course Hours:H(3-3) Prerequisite(s): Completion of at least 9 full-course equivalents and consent of the Department. Notes: Students completing a typical course sequence in their program would normally be eligible to enroll in their 3rd or 4th year. After consultation with a departmental faculty member who will supervise the chosen problem, a permission form obtained from the department office or website must be signed by the course supervisor before a student can register. MAY BE REPEATED FOR CREDIT
Original and independent thought, practical research and the completion of written and oral reports. Course Hours:F(0-6) Prerequisite(s): Completion of at least 15 full-course equivalents and consent of the Department. Notes: After consultation with a departmental faculty member who will supervise the chosen problem, a permission form obtained from the department office or website must be signed by the course supervisor before a student can register. MAY BE REPEATED FOR CREDIT
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. Course Hours:F(0-8) Prerequisite(s): Completion of at least 15 full-course equivalents and consent of the Department. Notes: After consultation with a department faculty member who will supervise the chosen problem, a permission form obtained from the department office or website must be completed before a student can register.
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. Course Hours:H(3-0) Prerequisite(s):Biochemistry 393or443, andChemistry 353or355.
Principles of signal transduction with examples from prokaryotes and eukaryotes. Discussion of protein covalent modifications, inositol lipid signaling, structure and function of protein kinases and protein phosphatases and their role in regulating various aspects of cell function. Emphasis on metabolic pathways, cell cycle control, checkpoints, DNA damage response and epigenetics. Course Hours:H(3-0) Prerequisite(s):Biochemistry 393or443.
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. Course Hours:H(3-0) Prerequisite(s): One of Biochemistry 341or393, andoneofBiochemistry 471orChemistry 371.
The material examines the structure and function of biological membranes with a strong emphasis on the role of membrane proteins. Topics may include: the physical properties of lipid bilayers, isolation and purification of membrane proteins, preparation of membrane mimetic systems, ion and solute movement across membranes (transport and ion channels), membrane protein folding, assembly and structure, and protein secretion and translocation systems. Course Hours:H(3-1T-0) Prerequisite(s):Biochemistry 393or443. Notes: Prior or concurrent completion of Biochemistry 431and471 is strongly recommended.
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. Course Hours:H(2-3T) Prerequisite(s):Biochemistry 393. Notes: Prior completion of Cellular, Molecular and Microbial Biology 411orBiochemistry 401 is strongly recommended. Also known as:(formerly Biotechnology 561)
Structure and function of lipids including phospholipids, sphingolipids, and steroids. Topics include properties of lipids and bilayers, lipid-lipid and lipid-protein interactions, technological applications, biosynthesis and regulation, lipids as second messengers, intracellular trafficking, and lipids in physiology and disease. Literature review and student seminars are significant components of this course. Course Hours:H(3-2T-0) Prerequisite(s):Biochemistry 393or443.
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. Course Hours:H(3-4/2) Prerequisite(s): One of Biochemistry 341or393andoneofBiochemistry 471orChemistry 371.
Enrolment 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
Selected Topics in Biochemistry
Selected topics in Biochemistry such as those which appear annually in the serial publication Annual Review of Biochemistry. Course Hours:H(3-0) MAY BE REPEATED FOR CREDIT
Contemporary methods of recombinant DNA technology will be combined with modern methods and strategies for expressing, secreting, purifying and characterizing proteins. This will include biophysical techniques, structural analysis and covalent modifications. Various modern 'omics' research approaches will also be discussed. Course Hours:H(3-0)
COURSES OF INSTRUCTION