Chemistry

The course introduces the basic principles of chemical analysis. The principles of chemical measurement, including error analysis, quality assurance and calibration, data acquisition and processing, are discussed with reference to methods of chemical analysis that are based on chemical equilibrium and stoichiometric reactions. The laboratory classes includes experiments demonstrating modern approaches of data acquisition and processing as well as chemical analysis based on chemical equilibrium. Prerequisites: Pass in CHEM1042; and Pass in CHEM1043, or already enrolled in this course.

The course provides students with an understanding of the pharmacological actions of a selection of the main classes of drugs in current therapeutic use. Lectures provide insight into the use of drugs in the treatment of a variety of human diseases ranging from cardiovascular and respiratory disease, through to inflammation, allergy, and pain. The drug treatment of the diseases is considered against the backdrop of the underlying disease processes, focusing primarily on the mechanisms by which the drugs bring about therapeutic relief. 

The course covers major advances, historical developments and contemporary applications of critical concepts in Chemistry. These may range from atomic theory and identification and arrangement of the elements to modern problems such as CO2 and global warming, pollution, and environmental clean-up. It focuses on the background to our knowledge, on what experimental evidence our current theories are based, and how old ones were overturned or modified. For science students in their third or fourth year of study under the four-year degree only. Other students with the prerequisites may seek instructor's approval for enrollment in the course.

This course provides an overview of a wide range of analysis methods for biomolecules (mostly biological macromolecules) such as proteins and DNA/RNA, and covers methods of current research of diverse fields in biochemistry 

Topics include Biomolecules, Preparation/separation (chromatography, electrophoresis), Detection (western blot, IP, ELISA, etc.), Imaging I (fluorescence, super resolution, AFM), Scattering (SAXS, DLS), Sequencing (NCS, single cell sequencing), Mass spectrometry, Structure determination (X-ray crystallography, Cryo-EM), Interaction (SPR, ITC), Single molecule techniques (FRET, magnetic tweezer. 

While there are no prerequisites for the course, coursework in Biochemistry I, Physical Chemistry I & II may be helpful. 

This course introduces the principles of 3D structures of proteins, which underlie all protein function, as well as the techniques used to obtain and analyze protein structures. The course strongly emphasizes protein dynamics as well; i.e. how protein structural flexibility permits enzymatic/receptor/structural activity. Finally, the course provides hands-on experience for all students, with in-silico analysis of protein structure, motion, and activity. 

The course provides an overview of the field of protein biophysics and structure, with a strong emphasis on practical analysis and structural evaluation. 

This course introduces undergraduate students to the labs in the chemistry department. Through the lab visit experience as a small group, students learn the diverse aspects of research in cutting-edge chemistry. Groups will visit 9 labs. Students produce two term-reports and a summary regarding lab visits. 

This course covers an overview of solid-state microanalysis methods, including elastic and inelastic scattering, identification of phases by morphology, chemical composition, electron diffraction, and microscopy. Principles and functions of different types of microscopes for materials analysis as well as spectroscopy for elemental analysis, analysis of spectra are also reviewed. Methods for surface analysis: Atomic force microscopy, scanning tunnelling microscopy, LEED, X-ray photoelectron spectroscopy (XPS) are covered.

This course examines the basic principles of pharmacology with an emphasis on drug action from the molecular and cellular levels to tissue, organ and whole organism levels. It will provide an understanding of the principles of drug action (pharmacodynamics) in terms of drug chemistry, drug-receptor interaction, receptor theory and dose-response relationships. An introduction to receptor-mediated signal transduction, membrane receptors and autonomic pharmacology will be covered. The handling of drugs by the body through the processes of absorption, distribution, metabolism and excretion (pharmacokinetics) will be covered in some detail along with drug analysis and the adverse effects of drugs. 

This course covers modern spectroscopic techniques used for structure elucidation of organic compounds and spectral data analysis techniques. 

Lectures on natural products biosynthesis and structure determination will be given at the end of the course.  

This course is specifically designed for students who will be practicing the structure determination of organic molecules for their research project. 

Topics include Basic Principles of NMR I, Basic Principles of NMR II; NMR Chemical Shift, Proton NMR (Mosher Ester Analysis + CASA reagent); Coupling Constants, Murata J-Based Method; Nonclassical Coupling + NMR Calculations, 2D NMR I (COSY, HSQC, HMBC); 2D NMR II (Other NMR Techniques), 2D NMR Peak Assignment Practice; 2D NMR Unknown Determination; Mass Spec Ionization; Mass Spec Application + Analyzer, Mass Spec Fragmentation analysis I; Mass Spec Fragment Analysis II, IR Group Frequency; Practical X-ray microED (Video Lecture), Biosynthesis I Introduction; Biosynthesis II NRPS, Biosynthesis III PKS; Biosynthesis IV Terpenes + Alkaloids, Biosynthesis V Review.