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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.
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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.
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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.
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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.
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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.
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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.
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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.
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This course covers the basic tools for polymer synthesis and characterization as well as applications of polymers in various fields. Topics include: Introduction to polymers; Step growth polymerization: linear and non-linear; Chain growth polymerization: (controlled/free) radical and ionic; Polymer solutions/mixing/separation; Physical properties/characterization (GPC, NMR, MALDI-TOF MS, thermal and mechanical properties); Applications of polymers in drug delivery and regenerative medicine; Recycling of polymers and designing polymers for recycling; Practical work on polymer synthesis and characterization. There are 5 pillars of this course are: 1) polymer synthesis; 2) polymer characterization; 3) polymer behavior; 4) applications; 5) recycling and end-of life management of polymers. These pillars provide the tools to understand and design polymers for specific applications, taking into account the desired properties and the end-of-life management of the materials. The course is supplemented by a practical experiment to expose the students to real-case examples. Students are divided into groups, and each group is tasked to polymerize a specific monomer using a specific technique. The second part of the experiment is focused on characterization of the synthesized polymer. The aim of the practical is to further learn through experiment the kinetics of polymerization reactions and the characterization methods. Knowledge on elementary organic chemistry, elementary thermodynamics, elementary physics, elementary reaction kinetics is recommended.
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This course is an in-depth exploration of the mechanisms underlying inorganic and organometallic reactions, with a particular focus on understanding their fundamentals and applications. Students examine key aspects of organometallic chemistry, including bonding, reactivity, and catalytic cycles, while also delving into spectroscopic and non-spectroscopic techniques used to probe reaction mechanisms. Techniques such as NMR, IR, UV-Vis spectroscopy, and kinetic studies are emphasized to elucidate reaction pathways and intermediate characterization. The course also highlights cutting-edge trends in inorganic and organometallic chemistry, showcasing recent advancements in catalysis and chemical transformations. By the end of the semester, students will develop a strong foundation in mechanistic analysis and contemporary methodologies used in inorganic chemistry research. CH344 is recommended as a prerequisite course. All lectures will be in English.
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This course introduces important instrumental techniques used in analytical chemistry, including thermal analysis (TGA, DSC), chemical and elemental analysis (AAS, ICP-AES, AFS, UV-visible absorption, FTIR, ATR-IR), Raman techniques, x-ray techniques (XFS, XPS, XRD), imaging and electron microscopy (SEM, TEM), mass spectrometry and its hyphenated techniques (GC-MS, MALDI). Case studies and real application examples in quality control, environmental analysis, materials characterization, forensic studies, etc. are illustrated. Beginning from the fundamentals and connecting these to real applications, students learn to appreciate the plethora of scientific tools developed to provide analysis solutions for real problems they encounter.
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