BCH210H1
U of T
Course Overview
Grade Boosters
Lessons & Practice
1. Fundamental Interactions
44min2. pH and Buffers
35min3. Amino Acid Structures
1.2hr4. Amino Acid Properties
1.3hr5. Protein Structure and Folding
20min6. Protein Purification and Identification
36min7. Studying Protein Structure
37min7.2.1. X-ray Crystallography7.2.2. Electron Microscopy7.2.3. Nuclear magnetic resonance (NMR)7.2.4. Infrared spectroscopy (IR)7.2.5. Circular Dichroism (CD)7.2.6. Example: Methods for Determining Protein Structure7.2.7. Example: Determining Structure of Small Protein7.2.8. Practice: Match the Protein to the Technique7.2.9. Example: Affinity Tag Chromatography
8. Functional Studies
14min9. Enzymes + Kinetics
13min10. Kinetics (cont.)
44min11. Biological Lipids and Membranes
56min12. Membrane Protein Structure
25min12.1.1. Proteins in the Lipid Bilayer12.1.2. Peripheral Membrane Proteins12.1.3. Integral Membrane Proteins12.1.4. Measuring Hydrophobicity12.1.5. Membrane Protein Folding12.1.6. Practice: Peripheral Membrane Proteins12.1.7. Practice: Integral Membrane Proteins12.1.8. Practice: Hydropathy12.1.9. Practice: Integral Membrane Proteins
13. Membrane Protein Function
51min14. Introduction to Metabolism and Thermodynamics
41min15. Carbohydrate Structure
34min16. Carbohydrate Metabolism
19min17. Mitochondrial Bioenergetics: TCA Cycle
21min18. Mitochondrial Bioenergetics: ETC
41min19. Fat Metabolism: Beta Oxidation
13min20. Fat Metabolism: Fatty Acid Synthesis
11min21. Gluconeogenesis
13min22. Ketogenesis
5minMidterm Overview
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Course Notes


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