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Video Clips

RealVideo®
10:37 minutes (7:30 - 18:07)
Endergonic and exergonic reactions reflect changes in Gibbs free energy (δG). Enzymes lower activation energy to speed up reaction.
Prof. Robert Weinberg
Chemical reactions and energetics is helpful
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RealVideo®
6:49 minutes (20:31 - 27:20)
Proteins as enzymes/catalysts, structures, antibodies/immune responses, motors and machines. Movie on protein motors.
Prof. Penny Chisholm, Prof. Graham Walker, Dr. Julia Khodor, Dr. Michelle Mischke
None
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RealVideo®
4:44 minutes (42:35 - 47:19)
Effect of activation energy on reaction rate, and function of catalysts.
Prof. Penny Chisholm, Prof. Graham Walker, Dr. Julia Khodor, Dr. Michelle Mischke
None
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RealVideo®
7:31 minutes (2:00 - 9:31)
Characteristics of catalysts - specificity, function, binding pocket for substrates, and transition states. Example showing transfer of phosphate from ATP to glucose.
Prof. Penny Chisholm, Prof. Graham Walker, Dr. Julia Khodor, Dr. Michelle Mischke
None
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Audio Clips

RealVideo®
14:05 minutes (0:00 - 14:05)
Discussion of the structure and function of macromolecules, with a particular focus on enzymes/catalysts.
Prof. Tyler Jacks, Prof. Hazel Sive
Proteins, Thermodynamics
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RealVideo®
5:59 minutes (14:05 - 20:04)
Energetics of reactants and products, and activation energy. Enzymes as biological catalysts and transition state complex. Nomenclature used in enzymatic reactions involving S (substrate/reactant), E (enzyme), ES (transition state), and P (product).
Prof. Tyler Jacks, Prof. Hazel Sive
Thermodynamics
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RealVideo®
11:56 minutes (20:04 - 32:00)
Enzyme-substrate interaction due to physical (shape) and chemical (amino acid properties) complementarity between the active site and the substrate. Three ways activation energy can be lowered: Proximity/orientation, induced-fit, and donation of charges to substrates. Example: Sucrase, phenylalanine hydroxylase.
Prof. Tyler Jacks, Prof. Hazel Sive
Enzymes
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RealVideo®
10:55 minutes (32:00 - 42:55)
Multiple ways to regulate enzymes. pH regulation through side chain protonation; temperature regulation through protein structure; covalent modification through phosphorylation; cofactors and coenzymes.
Prof. Tyler Jacks, Prof. Hazel Sive
Enzymes
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RealVideo®
7:22 minutes (42:55 - 50:17)
Function and mechanism of enzyme activators and inhibitors. Positive and negative feedback loops in a metabolic pathway. Definition: Reversible, irreversible, competitive, non-competitive, allosteric regulation. Example: Cancer drug Gleevec (competitive kinase inhibitor).
Prof. Tyler Jacks, Prof. Hazel Sive
Enzymes
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Lecture Notes

PDF
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Page 1 to page 2
Chemical reactions are based on thermodynamics and kinetics. Free energy diagram shows the energy of reaction, and the effect of enzymes on the activation energy.
Prof. Robert Weinberg
None
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PDF
Page 3 to page 8
Definition of enzyme, catalyst, substrate, and active site. Free energy diagram and enzyme mechanism. Michaelis-Menten enzyme kinetics, Km and Vmax.
Prof. Penny Chisholm, Prof. Graham Walker, Dr. Julia Khodor, Dr. Michelle Mischke
None
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Practice Problems

PDF
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Problem 2 (page 3)
Chemical interactions between an enzyme and a substrate in its binding pocket.
Prof. Robert Weinberg
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PDF
All problem (All page)
Enzymes, catalytic pockets, and reaction energetics. Contains a figure of all amino acid side chains as well as single letter and triple letter abbreviations.
Prof. Robert Weinberg
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PDF
Problem B (page 1)
Free energy, energy storage, spontaneous reactions, and the use of biological catalysts.
Prof. Penny Chisholm, Prof. Graham Walker, Dr. Julia Khodor, Dr. Michelle Mischke
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PDF
Problem C (page 3)
Enzyme kinetics including calculation of rates, Vmax, and Km.
Prof. Penny Chisholm, Prof. Graham Walker, Dr. Julia Khodor, Dr. Michelle Mischke
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Exam Questions

PDF
Problem 3 (page 7)
Label parts of a basic free energy diagram and how enzymes change the diagram.
Prof. Penny Chisholm, Prof. Graham Walker, Dr. Julia Khodor, Dr. Michelle Mischke
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