|
Instruction offered by members of the Department of Biological Sciences in the Faculty of Science.
Department Head – R.M.R. Barclay
Students interested in taking Biochemistry courses are urged to read the advice in the Faculty of Science Program section of this Calendar.
†Limited amounts of non-scheduled class time involvement will be required for these 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 and life processes. Basic concepts of metabolism are introduced, focusing on the breakdown of carbohydrates for energy. The laboratory component reinforces learning of the lecture material, while teaching technical skills and the analysis and interpretation of experiments involving biochemical molecules.
Course Hours:
H(3-3/2)
Prerequisite(s):
Chemistry 351.
Antirequisite(s):
Credit for both Biochemistry 341 and 393 will not be allowed.
Notes:
Not open to majors in the Department of Biological Sciences or Natural Sciences concentrators in Biological Sciences.
|
| back to top | |
|
|
†Biochemistry
393
|
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: Overview of current biochemical techniques for studying proteins, enzymes and metabolic pathways.
Course Hours:
H(3-3/2)
Prerequisite(s):
Biology 311 or Medical Sciences 341 (BHSc students only), and Chemistry 351.
Antirequisite(s):
Credit for both Biochemistry 393 and 341 will not be allowed.
Notes:
Prior or concurrent completion of Biology 331 is strongly recommended. Biochemistry 393 and 443 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.
|
| back to top | |
|
|
Biochemistry
401
|
Biochemistry Laboratory Techniques I
|
|
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 353 or 355; and Biochemistry 393.
Antirequisite(s):
Credit for both Biochemistry 401 and either 541 or Cellular, 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.
|
| back to top | |
|
|
Biochemistry
403
|
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.
Course Hours:
H(3-6)
Prerequisite(s):
Chemistry 311, Biochemistry 401 and 471.
Antirequisite(s):
Credit for both Biochemistry 403 and 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.
|
| back to top | |
|
|
Biochemistry
431
|
Proteins and Proteomics
|
|
Protein structure and chemistry: structural motifs, ligand-binding, conformational changes, chemical modification; protein folding; structure prediction by molecular modelling. 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 393 and one of Chemistry 353 or 355.
Antirequisite(s):
Credit for both Biochemistry 431 and 531 will not be allowed.
|
| back to top | |
|
|
Biochemistry
443
|
Metabolism and basic nucleic acid biochemistry
|
|
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 353 or 355; and Biochemistry 341 or 393.
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 program. Biochemistry 393 and 443 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.
|
| back to top | |
|
|
Biochemistry
471
|
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, and infrared as applied to biological molecules.
Course Hours:
H(3-2T)
Prerequisite(s):
Biochemistry 341 or 393; Chemistry 353 or 355; one of Mathematics 249, 251, 281, or Applied Mathematics 217 and one of Mathematics 253, 267, 277, 283, 211, 213, or Applied Mathematics 219; and Physics 211 or 221, and 223.
|
| back to top | |
|
|
Biochemistry
507
|
Special Problems in Biochemistry
|
|
Independent research or reading project that may include seminars, lectures, term papers and training in theoretical and/or laboratory methods.
Course Hours:
H(0-8) or H(3-0)
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 enrol 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
|
| back to top | |
|
|
Biochemistry
528
|
Independent Studies in Biochemistry
|
|
Original and independent thought, practical research and the completion of written and oral reports.
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 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
|
| back to top | |
|
|
Biochemistry
530
|
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.
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.
|
| back to top | |
|
|
Biochemistry
543
|
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.
Course Hours:
H(3-0)
Prerequisite(s):
Biochemistry 393 or 443, and Chemistry 353 or 355.
|
| back to top | |
|
|
Biochemistry
547
|
Signal Transduction and Regulation of Metabolism
|
|
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 393 or 443.
|
| back to top | |
|
|
Biochemistry
551
|
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.
Course Hours:
H(3-0)
Prerequisite(s):
One of Biochemistry 341 or 393, and one of Biochemistry 471 or Chemistry 371.
|
| back to top | |
|
|
Biochemistry
553
|
Molecular Biophysics
|
|
A comprehensive survey of modern biophysics covering the flow and processing of matter, energy and information in living systems. Equilibrium and non-equilibrium thermodynamics in biology. Molecular motors and facilitated proton transport. An integrative approach connecting atomistic theories to cellular processes.
Course Hours:
H(3-0)
Prerequisite(s):
Biochemistry 341 or 393; and Biochemistry 471 or Chemistry 371.
Notes:
Prior completion of Biochemistry 555 is strongly recommended.
Also known as:
(formerly Biology 553)
|
| back to top | |
|
|
Biochemistry
555
|
Biomembranes
|
|
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 393 or 443.
Notes:
Prior or concurrent completion of Biochemistry 431 and 471 is strongly recommended.
|
| back to top | |
|
|
Biochemistry
561
|
Applied Biochemistry and Biotechnology
|
|
An introduction to the language, materials, methods, concepts and commercial applications of biotechnology with emphasis on methodology, biocatalysts, and key concepts of genome sequencing, proteomics, and transcriptomics. Also, drug and antibiotic development, mechanisms of some drugs, and drug resistance will be introduced.
Course Hours:
H(3-0)
Prerequisite(s):
Biochemistry 393.
Antirequisite(s):
Credit for both Biochemistry 561 and Biotechnology 561 will not be allowed.
Notes:
Prior completion of Cellular, Molecular and Microbial Biology 411 or Biochemistry 401 is strongly recommended.
|
| back to top | |
|
|
|
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(3-1T-0)
Prerequisite(s):
Biochemistry 393 or 443.
|
| back to top | |
|
|
Biochemistry
577
|
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.
Course Hours:
H(3-4)
Prerequisite(s):
One of Biochemistry 341 or 393 and one of Biochemistry 471 or Chemistry 371.
|
| back to top | |
|
Graduate Courses
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
|
| back to top | |
|
|
Biochemistry
731
|
Current Topics in Biochemistry
|
|
A discussion of contemporary experimental and theoretical biochemical methods used for the study of drugs and diagnostics at a molecular level. Structural analysis, drug design and molecular dynamics methods will be described, as well as current practices for commercialization. Various modern 'omics' research approaches and current leading drug targets of the pharmaceutical industry will also be discussed.
Course Hours:
H(3-0)
|
| back to top | |
|
COURSES OF INSTRUCTION