

Raffi Hovasapian
Enzymes IV: Lineweaver-Burk Plots
Slide Duration:Table of Contents
Section 1: Preliminaries on Aqueous Chemistry
Aqueous Solutions & Concentration
39m 57s
- Intro0:00
- Aqueous Solutions and Concentration0:46
- Definition of Solution1:28
- Example: Sugar Dissolved in Water2:19
- Example: Salt Dissolved in Water3:04
- A Solute Does Not Have to Be a Solid3:37
- A Solvent Does Not Have to Be a Liquid5:02
- Covalent Compounds6:55
- Ionic Compounds7:39
- Example: Table Sugar9:12
- Example: MgCl₂10:40
- Expressing Concentration: Molarity13:42
- Example 114:47
- Example 1: Question14:50
- Example 1: Solution15:40
- Another Way to Express Concentration22:01
- Example 224:00
- Example 2: Question24:01
- Example 2: Solution24:49
- Some Other Ways of Expressing Concentration27:52
- Example 329:30
- Example 3: Question29:31
- Example 3: Solution31:02
Dilution & Osmotic Pressure
38m 53s
- Intro0:00
- Dilution0:45
- Definition of Dilution0:46
- Example 1: Question2:08
- Example 1: Basic Dilution Equation4:20
- Example 1: Solution5:31
- Example 2: Alternative Approach12:05
- Osmotic Pressure14:34
- Colligative Properties15:02
- Recall: Covalent Compounds and Soluble Ionic Compounds17:24
- Properties of Pure Water19:42
- Addition of a Solute21:56
- Osmotic Pressure: Conceptual Example24:00
- Equation for Osmotic Pressure29:30
- Example of 'i'31:38
- Example 332:50
More on Osmosis
29m 1s
- Intro0:00
- More on Osmosis1:25
- Osmotic Pressure1:26
- Example 1: Molar Mass of Protein5:25
- Definition, Equation, and Unit of Osmolarity13:13
- Example 2: Osmolarity15:19
- Isotonic, Hypertonic, and Hypotonic20:20
- Example 322:20
- More on Isotonic, Hypertonic, and Hypotonic26:14
- Osmosis vs. Osmotic Pressure27:56
Acids & Bases
39m 11s
- Intro0:00
- Acids and Bases1:16
- Let's Begin With H₂O1:17
- P-Scale4:22
- Example 16:39
- pH9:43
- Strong Acids11:10
- Strong Bases13:52
- Weak Acids & Bases Overview14:32
- Weak Acids15:49
- Example 2: Phosphoric Acid19:30
- Weak Bases24:50
- Weak Base Produces Hydroxide Indirectly25:41
- Example 3: Pyridine29:07
- Acid Form and Base Form32:02
- Acid Reaction35:50
- Base Reaction36:27
- Ka, Kb, and Kw37:14
Titrations and Buffers
41m 33s
- Intro0:00
- Titrations0:27
- Weak Acid0:28
- Rearranging the Ka Equation1:45
- Henderson-Hasselbalch Equation3:52
- Fundamental Reaction of Acids and Bases5:36
- The Idea Behind a Titration6:27
- Let's Look at an Acetic Acid Solution8:44
- Titration Curve17:00
- Acetate23:57
- Buffers26:57
- Introduction to Buffers26:58
- What is a Buffer?29:40
- Titration Curve & Buffer Region31:44
- How a Buffer Works: Adding OH⁻34:44
- How a Buffer Works: Adding H⁺35:58
- Phosphate Buffer System38:02
Example Problems with Acids, Bases & Buffers
44m 19s
- Intro0:00
- Example 11:21
- Example 1: Properties of Glycine1:22
- Example 1: Part A3:40
- Example 1: Part B4:40
- Example 29:02
- Example 2: Question9:03
- Example 2: Total Phosphate Concentration12:23
- Example 2: Final Solution17:10
- Example 319:34
- Example 3: Question19:35
- Example 3: pH Before22:18
- Example 3: pH After24:24
- Example 3: New pH27:54
- Example 430:00
- Example 4: Question30:01
- Example 4: Equilibria32:52
- Example 4: 1st Reaction38:04
- Example 4: 2nd Reaction39:53
- Example 4: Final Solution41:33
Hydrolysis & Condensation Reactions
18m 45s
- Intro0:00
- Hydrolysis and Condensation Reactions0:50
- Hydrolysis0:51
- Condensation2:42
- Example 1: Hydrolysis of Ethyl Acetate4:52
- Example 2: Condensation of Acetic Acid with Ethanol8:42
- Example 311:18
- Example 4: Formation & Hydrolysis of a Peptide Bond Between the Amino Acids Alanine & Serine14:56
Section 2: Amino Acids & Proteins: Primary Structure
Amino Acids
38m 19s
- Intro0:00
- Amino Acids0:17
- Proteins & Amino Acids0:18
- Difference Between Amino Acids4:20
- α-Carbon7:08
- Configuration in Biochemistry10:43
- L-Glyceraldehyde & Fischer Projection12:32
- D-Glyceraldehyde & Fischer Projection15:31
- Amino Acids in Biological Proteins are the L Enantiomer16:50
- L-Amino Acid18:04
- L-Amino Acids Correspond to S-Enantiomers in the RS System20:10
- Classification of Amino Acids22:53
- Amino Acids With Non-Polar R Groups26:45
- Glycine27:00
- Alanine27:48
- Valine28:15
- Leucine28:58
- Proline31:08
- Isoleucine32:42
- Methionine33:43
- Amino Acids With Aromatic R Groups34:33
- Phenylalanine35:26
- Tyrosine36:02
- Tryptophan36:32
Amino Acids, Continued
27m 14s
- Intro0:00
- Amino Acids With Positively Charged R Groups0:16
- Lysine0:52
- Arginine1:55
- Histidine3:15
- Amino Acids With Negatively Charged R Groups6:28
- Aspartate6:58
- Glutamate8:11
- Amino Acids With Uncharged, but Polar R Groups8:50
- Serine8:51
- Threonine10:21
- Cysteine11:06
- Asparagine11:35
- Glutamine12:44
- More on Amino Acids14:18
- Cysteine Dimerizes to Form Cystine14:53
- Tryptophan, Tyrosine, and Phenylalanine19:07
- Other Amino Acids20:53
- Other Amino Acids: Hydroxy Lysine22:34
- Other Amino Acids: r-Carboxy Glutamate25:37
Acid/Base Behavior of Amino Acids
48m 28s
- Intro0:00
- Acid/Base Behavior of Amino Acids0:27
- Acid/Base Behavior of Amino Acids0:28
- Let's Look at Alanine1:57
- Titration of Acidic Solution of Alanine with a Strong Base2:51
- Amphoteric Amino Acids13:24
- Zwitterion & Isoelectric Point16:42
- Some Amino Acids Have 3 Ionizable Groups20:35
- Example: Aspartate24:44
- Example: Tyrosine28:50
- Rule of Thumb33:04
- Basis for the Rule35:59
- Example: Describe the Degree of Protonation for Each Ionizable Group38:46
- Histidine is Special44:58
Peptides & Proteins
45m 18s
- Intro0:00
- Peptides and Proteins0:15
- Introduction to Peptides and Proteins0:16
- Formation of a Peptide Bond: The Bond Between 2 Amino Acids1:44
- Equilibrium7:53
- Example 1: Build the Following Tripeptide Ala-Tyr-Ile9:48
- Example 1: Shape Structure15:43
- Example 1: Line Structure17:11
- Peptides Bonds20:08
- Terms We'll Be Using Interchangeably23:14
- Biological Activity & Size of a Peptide24:58
- Multi-Subunit Proteins30:08
- Proteins and Prosthetic Groups32:13
- Carbonic Anhydrase37:35
- Primary, Secondary, Tertiary, and Quaternary Structure of Proteins40:26
Amino Acid Sequencing of a Peptide Chain
42m 47s
- Intro0:00
- Amino Acid Sequencing of a Peptide Chain0:30
- Amino Acid Sequence and Its Structure0:31
- Edman Degradation: Overview2:57
- Edman Degradation: Reaction - Part 14:58
- Edman Degradation: Reaction - Part 210:28
- Edman Degradation: Reaction - Part 313:51
- Mechanism Step 1: PTC (Phenylthiocarbamyl) Formation19:01
- Mechanism Step 2: Ring Formation & Peptide Bond Cleavage23:03
- Example: Write Out the Edman Degradation for the Tripeptide Ala-Tyr-Ser30:29
- Step 130:30
- Step 234:21
- Step 336:56
- Step 438:28
- Step 539:24
- Step 640:44
Sequencing Larger Peptides & Proteins
1h 2m 33s
- Intro0:00
- Sequencing Larger Peptides and Proteins0:28
- Identifying the N-Terminal Amino Acids With the Reagent Fluorodinitrobenzene (FDNB)0:29
- Sequencing Longer Peptides & Proteins Overview5:54
- Breaking Peptide Bond: Proteases and Chemicals8:16
- Some Enzymes/Chemicals Used for Fragmentation: Trypsin11:14
- Some Enzymes/Chemicals Used for Fragmentation: Chymotrypsin13:02
- Some Enzymes/Chemicals Used for Fragmentation: Cyanogen Bromide13:28
- Some Enzymes/Chemicals Used for Fragmentation: Pepsin13:44
- Cleavage Location14:04
- Example: Chymotrypsin16:44
- Example: Pepsin18:17
- More on Sequencing Larger Peptides and Proteins19:29
- Breaking Disulfide Bonds: Performic Acid26:08
- Breaking Disulfide Bonds: Dithiothreitol Followed by Iodoacetate31:04
- Example: Sequencing Larger Peptides and Proteins37:03
- Part 1 - Breaking Disulfide Bonds, Hydrolysis and Separation37:04
- Part 2 - N-Terminal Identification44:16
- Part 3 - Sequencing Using Pepsin46:43
- Part 4 - Sequencing Using Cyanogen Bromide52:02
- Part 5 - Final Sequence56:48
Peptide Synthesis (Merrifield Process)
49m 12s
- Intro0:00
- Peptide Synthesis (Merrifield Process)0:31
- Introduction to Synthesizing Peptides0:32
- Merrifield Peptide Synthesis: General Scheme3:03
- So What Do We Do?6:07
- Synthesis of Protein in the Body Vs. The Merrifield Process7:40
- Example: Synthesis of Ala-Gly-Ser9:21
- Synthesis of Ala-Gly-Ser: Reactions Overview11:41
- Synthesis of Ala-Gly-Ser: Reaction 119:34
- Synthesis of Ala-Gly-Ser: Reaction 224:34
- Synthesis of Ala-Gly-Ser: Reaction 327:34
- Synthesis of Ala-Gly-Ser: Reaction 4 & 4a28:48
- Synthesis of Ala-Gly-Ser: Reaction 533:38
- Synthesis of Ala-Gly-Ser: Reaction 636:45
- Synthesis of Ala-Gly-Ser: Reaction 7 & 7a37:44
- Synthesis of Ala-Gly-Ser: Reaction 839:47
- Synthesis of Ala-Gly-Ser: Reaction 9 & 1043:23
- Chromatography: Eluent, Stationary Phase, and Eluate45:55
More Examples with Amino Acids & Peptides
54m 31s
- Intro0:00
- Example 10:22
- Data0:23
- Part A: What is the pI of Serine & Draw the Correct Structure2:11
- Part B: How Many mL of NaOH Solution Have Been Added at This Point (pI)?5:27
- Part C: At What pH is the Average Charge on Serine10:50
- Part D: Draw the Titration Curve for This Situation14:50
- Part E: The 10 mL of NaOH Added to the Solution at the pI is How Many Equivalents?17:35
- Part F: Serine Buffer Solution20:22
- Example 223:04
- Data23:05
- Part A: Calculate the Minimum Molar Mass of the Protein25:12
- Part B: How Many Tyr Residues in this Protein?28:34
- Example 330:08
- Question30:09
- Solution34:30
- Example 448:46
- Question48:47
- Solution49:50
Section 3: Proteins: Secondary, Tertiary, and Quaternary Structure
Alpha Helix & Beta Conformation
50m 52s
- Intro0:00
- Alpha Helix and Beta Conformation0:28
- Protein Structure Overview0:29
- Weak interactions Among the Amino Acid in the Peptide Chain2:11
- Two Principals of Folding Patterns4:56
- Peptide Bond7:00
- Peptide Bond: Resonance9:46
- Peptide Bond: φ Bond & ψ Bond11:22
- Secondary Structure15:08
- α-Helix Folding Pattern17:28
- Illustration 1: α-Helix Folding Pattern19:22
- Illustration 2: α-Helix Folding Pattern21:39
- β-Sheet25:16
- β-Conformation26:04
- Parallel & Anti-parallel28:44
- Parallel β-Conformation Arrangement of the Peptide Chain30:12
- Putting Together a Parallel Peptide Chain35:16
- Anti-Parallel β-Conformation Arrangement37:42
- Tertiary Structure45:03
- Quaternary Structure45:52
- Illustration 3: Myoglobin Tertiary Structure & Hemoglobin Quaternary Structure47:13
- Final Words on Alpha Helix and Beta Conformation48:34
Section 4: Proteins: Function
Protein Function I: Ligand Binding & Myoglobin
51m 36s
- Intro0:00
- Protein Function I: Ligand Binding & Myoglobin0:30
- Ligand1:02
- Binding Site2:06
- Proteins are Not Static or Fixed3:36
- Multi-Subunit Proteins5:46
- O₂ as a Ligand7:21
- Myoglobin, Protoporphyrin IX, Fe ²⁺, and O₂12:54
- Protoporphyrin Illustration14:25
- Myoglobin With a Heme Group Illustration17:02
- Fe²⁺ has 6 Coordination Sites & Binds O₂18:10
- Heme19:44
- Myoglobin Overview22:40
- Myoglobin and O₂ Interaction23:34
- Keq or Ka & The Measure of Protein's Affinity for Its Ligand26:46
- Defining α: Fraction of Binding Sites Occupied32:52
- Graph: α vs. [L]37:33
- For The Special Case of α = 0.539:01
- Association Constant & Dissociation Constant43:54
- α & Kd45:15
- Myoglobin's Binding of O₂48:20
Protein Function II: Hemoglobin
1h 3m 36s
- Intro0:00
- Protein Function II: Hemoglobin0:14
- Hemoglobin Overview0:15
- Hemoglobin & Its 4 Subunits1:22
- α and β Interactions5:18
- Two Major Conformations of Hb: T State (Tense) & R State (Relaxed)8:06
- Transition From The T State to R State12:03
- Binding of Hemoglobins & O₂14:02
- Binding Curve18:32
- Hemoglobin in the Lung27:28
- Signoid Curve30:13
- Cooperative Binding32:25
- Hemoglobin is an Allosteric Protein34:26
- Homotropic Allostery36:18
- Describing Cooperative Binding Quantitatively38:06
- Deriving The Hill Equation41:52
- Graphing the Hill Equation44:43
- The Slope and Degree of Cooperation46:25
- The Hill Coefficient49:48
- Hill Coefficient = 151:08
- Hill Coefficient < 155:55
- Where the Graph Hits the x-axis56:11
- Graph for Hemoglobin58:02
Protein Function III: More on Hemoglobin
1h 7m 16s
- Intro0:00
- Protein Function III: More on Hemoglobin0:11
- Two Models for Cooperative Binding: MWC & Sequential Model0:12
- MWC Model1:31
- Hemoglobin Subunits3:32
- Sequential Model8:00
- Hemoglobin Transports H⁺ & CO₂17:23
- Binding Sites of H⁺ and CO₂19:36
- CO₂ is Converted to Bicarbonate23:28
- Production of H⁺ & CO₂ in Tissues27:28
- H⁺ & CO₂ Binding are Inversely Related to O₂ Binding28:31
- The H⁺ Bohr Effect: His¹⁴⁶ Residue on the β Subunits33:31
- Heterotropic Allosteric Regulation of O₂ Binding by 2,3-Biphosphoglycerate (2,3 BPG)39:53
- Binding Curve for 2,3 BPG56:21
Section 5: Enzymes
Enzymes I
41m 38s
- Intro0:00
- Enzymes I0:38
- Enzymes Overview0:39
- Cofactor4:38
- Holoenzyme5:52
- Apoenzyme6:40
- Riboflavin, FAD, Pyridoxine, Pyridoxal Phosphate Structures7:28
- Carbonic Anhydrase8:45
- Classification of Enzymes9:55
- Example: EC 1.1.1.113:04
- Reaction of Oxidoreductases16:23
- Enzymes: Catalysts, Active Site, and Substrate18:28
- Illustration of Enzymes, Substrate, and Active Site27:22
- Catalysts & Activation Energies29:57
- Intermediates36:00
Enzymes II
44m 2s
- Intro0:00
- Enzymes II: Transitions State, Binding Energy, & Induced Fit0:18
- Enzymes 'Fitting' Well With The Transition State0:20
- Example Reaction: Breaking of a Stick3:40
- Another Energy Diagram8:20
- Binding Energy9:48
- Enzymes Specificity11:03
- Key Point: Optimal Interactions Between Substrate & Enzymes15:15
- Induced Fit16:25
- Illustrations: Induced Fit20:58
- Enzymes II: Catalytic Mechanisms22:17
- General Acid/Base Catalysis23:56
- Acid Form & Base Form of Amino Acid: Glu &Asp25:26
- Acid Form & Base Form of Amino Acid: Lys & Arg26:30
- Acid Form & Base Form of Amino Acid: Cys26:51
- Acid Form & Base Form of Amino Acid: His27:30
- Acid Form & Base Form of Amino Acid: Ser28:16
- Acid Form & Base Form of Amino Acid: Tyr28:30
- Example: Phosphohexose Isomerase29:20
- Covalent Catalysis34:19
- Example: Glyceraldehyde 3-Phosphate Dehydrogenase35:34
- Metal Ion Catalysis: Isocitrate Dehydrogenase38:45
- Function of Mn²⁺42:15
Enzymes III: Kinetics
56m 40s
- Intro0:00
- Enzymes III: Kinetics1:40
- Rate of an Enzyme-Catalyzed Reaction & Substrate Concentration1:41
- Graph: Substrate Concentration vs. Reaction Rate10:43
- Rate At Low and High Substrate Concentration14:26
- Michaelis & Menten Kinetics20:16
- More On Rate & Concentration of Substrate22:46
- Steady-State Assumption26:02
- Rate is Determined by How Fast ES Breaks Down to Product31:36
- Total Enzyme Concentration: [Et] = [E] + [ES]35:35
- Rate of ES Formation36:44
- Rate of ES Breakdown38:40
- Measuring Concentration of Enzyme-Substrate Complex41:19
- Measuring Initial & Maximum Velocity43:43
- Michaelis & Menten Equation46:44
- What Happens When V₀ = (1/2) Vmax?49:12
- When [S] << Km53:32
- When [S] >> Km54:44
Enzymes IV: Lineweaver-Burk Plots
20m 37s
- Intro0:00
- Enzymes IV: Lineweaver-Burk Plots0:45
- Deriving The Lineweaver-Burk Equation0:46
- Lineweaver-Burk Plots3:55
- Example 1: Carboxypeptidase A8:00
- More on Km, Vmax, and Enzyme-catalyzed Reaction15:54
Enzymes V: Enzyme Inhibition
51m 37s
- Intro0:00
- Enzymes V: Enzyme Inhibition Overview0:42
- Enzyme Inhibitors Overview0:43
- Classes of Inhibitors2:32
- Competitive Inhibition3:08
- Competitive Inhibition3:09
- Michaelis & Menten Equation in the Presence of a Competitive Inhibitor7:40
- Double-Reciprocal Version of the Michaelis & Menten Equation14:48
- Competitive Inhibition Graph16:37
- Uncompetitive Inhibition19:23
- Uncompetitive Inhibitor19:24
- Michaelis & Menten Equation for Uncompetitive Inhibition22:10
- The Lineweaver-Burk Equation for Uncompetitive Inhibition26:04
- Uncompetitive Inhibition Graph27:42
- Mixed Inhibition30:30
- Mixed Inhibitor30:31
- Double-Reciprocal Version of the Equation33:34
- The Lineweaver-Burk Plots for Mixed Inhibition35:02
- Summary of Reversible Inhibitor Behavior38:00
- Summary of Reversible Inhibitor Behavior38:01
- Note: Non-Competitive Inhibition42:22
- Irreversible Inhibition45:15
- Irreversible Inhibition45:16
- Penicillin & Transpeptidase Enzyme46:50
Enzymes VI: Regulatory Enzymes
51m 23s
- Intro0:00
- Enzymes VI: Regulatory Enzymes0:45
- Regulatory Enzymes Overview0:46
- Example: Glycolysis2:27
- Allosteric Regulatory Enzyme9:19
- Covalent Modification13:08
- Two Other Regulatory Processes16:28
- Allosteric Regulation20:58
- Feedback Inhibition25:12
- Feedback Inhibition Example: L-Threonine → L-Isoleucine26:03
- Covalent Modification27:26
- Covalent Modulators: -PO₃²⁻29:30
- Protein Kinases31:59
- Protein Phosphatases32:47
- Addition/Removal of -PO₃²⁻ and the Effect on Regulatory Enzyme33:36
- Phosphorylation Sites of a Regulatory Enzyme38:38
- Proteolytic Cleavage41:48
- Zymogens: Chymotrypsin & Trypsin43:58
- Enzymes That Use More Than One Regulatory Process: Bacterial Glutamine Synthetase48:59
- Why The Complexity?50:27
Enzymes VII: Km & Kcat
54m 49s
- Intro0:00
- Km1:48
- Recall the Michaelis–Menten Equation1:49
- Km & Enzyme's Affinity6:18
- Rate Forward, Rate Backward, and Equilibrium Constant11:08
- When an Enzyme's Affinity for Its Substrate is High14:17
- More on Km & Enzyme Affinity17:29
- The Measure of Km Under Michaelis–Menten kinetic23:19
- Kcat (First-order Rate Constant or Catalytic Rate Constant)24:10
- Kcat: Definition24:11
- Kcat & The Michaelis–Menten Postulate25:18
- Finding Vmax and [Et}27:27
- Units for Vmax and Kcat28:26
- Kcat: Turnover Number28:55
- Michaelis–Menten Equation32:12
- Km & Kcat36:37
- Second Order Rate Equation36:38
- (Kcat)/(Km): Overview39:22
- High (Kcat)/(Km)40:20
- Low (Kcat)/(Km)43:16
- Practical Big Picture46:28
- Upper Limit to (Kcat)/(Km)48:56
- More On Kcat and Km49:26
Section 6: Carbohydrates
Monosaccharides
1h 17m 46s
- Intro0:00
- Monosaccharides1:49
- Carbohydrates Overview1:50
- Three Major Classes of Carbohydrates4:48
- Definition of Monosaccharides5:46
- Examples of Monosaccharides: Aldoses7:06
- D-Glyceraldehyde7:39
- D-Erythrose9:00
- D-Ribose10:10
- D-Glucose11:20
- Observation: Aldehyde Group11:54
- Observation: Carbonyl 'C'12:30
- Observation: D & L Naming System12:54
- Examples of Monosaccharides: Ketose16:54
- Dihydroxy Acetone17:28
- D-Erythrulose18:30
- D-Ribulose19:49
- D-Fructose21:10
- D-Glucose Comparison23:18
- More information of Ketoses24:50
- Let's Look Closer at D-Glucoses25:50
- Let's Look At All the D-Hexose Stereoisomers31:22
- D-Allose32:20
- D-Altrose33:01
- D-Glucose33:39
- D-Gulose35:00
- D-Mannose35:40
- D-Idose36:42
- D-Galactose37:14
- D-Talose37:42
- Epimer40:05
- Definition of Epimer40:06
- Example of Epimer: D-Glucose, D-Mannose, and D-Galactose40:57
- Hemiacetal or Hemiketal44:36
- Hemiacetal/Hemiketal Overview45:00
- Ring Formation of the α and β Configurations of D-Glucose50:52
- Ring Formation of the α and β Configurations of Fructose1:01:39
- Haworth Projection1:07:34
- Pyranose & Furanose Overview1:07:38
- Haworth Projection: Pyranoses1:09:30
- Haworth Projection: Furanose1:14:56
Hexose Derivatives & Reducing Sugars
37m 6s
- Intro0:00
- Hexose Derivatives0:15
- Point of Clarification: Forming a Cyclic Sugar From a Linear Sugar0:16
- Let's Recall the α and β Anomers of Glucose8:42
- α-Glucose10:54
- Hexose Derivatives that Play Key Roles in Physiology Progression17:38
- β-Glucose18:24
- β-Glucosamine18:48
- N-Acetyl-β-Glucosamine20:14
- β-Glucose-6-Phosphate22:22
- D-Gluconate24:10
- Glucono-δ-Lactone26:33
- Reducing Sugars29:50
- Reducing Sugars Overview29:51
- Reducing Sugars Example: β-Galactose32:36
Disaccharides
43m 32s
- Intro0:00
- Disaccharides0:15
- Disaccharides Overview0:19
- Examples of Disaccharides & How to Name Them2:49
- Disaccharides Trehalose Overview15:46
- Disaccharides Trehalose: Flip20:52
- Disaccharides Trehalose: Spin28:36
- Example: Draw the Structure33:12
Polysaccharides
39m 25s
- Intro0:00
- Recap Example: Draw the Structure of Gal(α1↔β1)Man0:38
- Polysaccharides9:46
- Polysaccharides Overview9:50
- Homopolysaccharide13:12
- Heteropolysaccharide13:47
- Homopolysaccharide as Fuel Storage16:23
- Starch Has Two Types of Glucose Polymer: Amylose17:10
- Starch Has Two Types of Glucose Polymer: Amylopectin18:04
- Polysaccharides: Reducing End & Non-Reducing End19:30
- Glycogen20:06
- Examples: Structures of Polysaccharides21:42
- Let's Draw an (α1→4) & (α1→6) of Amylopectin by Hand.28:14
- More on Glycogen31:17
- Glycogen, Concentration, & The Concept of Osmolarity35:16
Polysaccharides, Part 2
44m 15s
- Intro0:00
- Polysaccharides0:17
- Example: Cellulose0:34
- Glycoside Bond7:25
- Example Illustrations12:30
- Glycosaminoglycans Part 115:55
- Glycosaminoglycans Part 218:34
- Glycosaminoglycans & Sulfate Attachments22:42
- β-D-N-Acetylglucosamine24:49
- β-D-N-AcetylGalactosamine25:42
- β-D-Glucuronate26:44
- β-L-Iduronate27:54
- More on Sulfate Attachments29:49
- Hylarunic Acid32:00
- Hyaluronates39:32
- Other Glycosaminoglycans40:46
Glycoconjugates
44m 23s
- Intro0:00
- Glycoconjugates0:24
- Overview0:25
- Proteoglycan2:53
- Glycoprotein5:20
- Glycolipid7:25
- Proteoglycan vs. Glycoprotein8:15
- Cell Surface Diagram11:17
- Proteoglycan Common Structure14:24
- Example: Chondroitin-4-Sulfate15:06
- Glycoproteins19:50
- The Monomers that Commonly Show Up in The Oligo Portions of Glycoproteins28:02
- N-Acetylneuraminic Acid31:17
- L-Furose32:37
- Example of an N-Linked Oligosaccharide33:21
- Cell Membrane Structure36:35
- Glycolipids & Lipopolysaccharide37:22
- Structure Example41:28
More Example Problems with Carbohydrates
40m 22s
- Intro0:00
- Example 11:09
- Example 22:34
- Example 35:12
- Example 416:19
- Question16:20
- Solution17:25
- Example 524:18
- Question24:19
- Structure of 2,3-Di-O-Methylglucose26:47
- Part A28:11
- Part B33:46
Section 7: Lipids
Fatty Acids & Triacylglycerols
54m 55s
- Intro0:00
- Fatty Acids0:32
- Lipids Overview0:34
- Introduction to Fatty Acid3:18
- Saturated Fatty Acid6:13
- Unsaturated or Polyunsaturated Fatty Acid7:07
- Saturated Fatty Acid Example7:46
- Unsaturated Fatty Acid Example9:06
- Notation Example: Chain Length, Degree of Unsaturation, & Double Bonds Location of Fatty Acid11:56
- Example 1: Draw the Structure16:18
- Example 2: Give the Shorthand for cis,cis-5,8-Hexadecadienoic Acid20:12
- Example 323:12
- Solubility of Fatty Acids25:45
- Melting Points of Fatty Acids29:40
- Triacylglycerols34:13
- Definition of Triacylglycerols34:14
- Structure of Triacylglycerols35:08
- Example: Triacylglycerols40:23
- Recall Ester Formation43:57
- The Body's Primary Fuel-Reserves47:22
- Two Primary Advantages to Storing Energy as Triacylglycerols Instead of Glycogen: Number 149:24
- Two Primary Advantages to Storing Energy as Triacylglycerols Instead of Glycogen: Number 251:54
Membrane Lipids
38m 51s
- Intro0:00
- Membrane Lipids0:26
- Definition of Membrane Lipids0:27
- Five Major Classes of Membrane Lipids2:38
- Glycerophospholipids5:04
- Glycerophospholipids Overview5:05
- The X Group8:05
- Example: Phosphatidyl Ethanolamine10:51
- Example: Phosphatidyl Choline13:34
- Phosphatidyl Serine15:16
- Head Groups16:50
- Ether Linkages Instead of Ester Linkages20:05
- Galactolipids23:39
- Galactolipids Overview23:40
- Monogalactosyldiacylglycerol: MGDG25:17
- Digalactosyldiacylglycerol: DGDG28:13
- Structure Examples 1: Lipid Bilayer31:35
- Structure Examples 2: Cross Section of a Cell34:56
- Structure Examples 3: MGDG & DGDG36:28
Membrane Lipids, Part 2
38m 20s
- Intro0:00
- Sphingolipids0:11
- Sphingolipid Overview0:12
- Sphingosine Structure1:42
- Ceramide3:56
- Subclasses of Sphingolipids Overview6:00
- Subclasses of Sphingolipids: Sphingomyelins7:53
- Sphingomyelins7:54
- Subclasses of Sphingolipids: Glycosphingolipid12:47
- Glycosphingolipid Overview12:48
- Cerebrosides & Globosides Overview14:33
- Example: Cerebrosides15:43
- Example: Globosides17:14
- Subclasses of Sphingolipids: Gangliosides19:07
- Gangliosides19:08
- Medical Application: Tay-Sachs Disease23:34
- Sterols30:45
- Sterols: Basic Structure30:46
- Important Example: Cholesterol32:01
- Structures Example34:13
The Biologically Active Lipids
48m 36s
- Intro0:00
- The Biologically Active Lipids0:44
- Phosphatidyl Inositol Structure0:45
- Phosphatidyl Inositol Reaction3:24
- Image Example12:49
- Eicosanoids14:12
- Arachidonic Acid & Membrane Lipid Containing Arachidonic Acid18:41
- Three Classes of Eicosanoids20:42
- Overall Structures21:38
- Prostagladins22:56
- Thromboxane27:19
- Leukotrienes30:19
- More On The Biologically Active Lipids33:34
- Steroid Hormones33:35
- Fat Soluble Vitamins38:25
- Vitamin D₃40:40
- Vitamin A43:17
- Vitamin E45:12
- Vitamin K47:17
Section 8: Energy & Biological Systems (Bioenergetics)
Thermodynamics, Free Energy & Equilibrium
45m 51s
- Intro0:00
- Thermodynamics, Free Energy and Equilibrium1:03
- Reaction: Glucose + Pi → Glucose 6-Phosphate1:50
- Thermodynamics & Spontaneous Processes3:31
- In Going From Reactants → Product, a Reaction Wants to Release Heat6:30
- A Reaction Wants to Become More Disordered9:10
- ∆H < 010:30
- ∆H > 010:57
- ∆S > 011:23
- ∆S <011:56
- ∆G = ∆H - T∆S at Constant Pressure12:15
- Gibbs Free Energy15:00
- ∆G < 016:49
- ∆G > 017:07
- Reference Frame For Thermodynamics Measurements17:57
- More On BioChemistry Standard22:36
- Spontaneity25:36
- Keq31:45
- Example: Glucose + Pi → Glucose 6-Phosphate34:14
- Example Problem 140:25
- Question40:26
- Solution41:12
More on Thermodynamics & Free Energy
37m 6s
- Intro0:00
- More on Thermodynamics & Free Energy0:16
- Calculating ∆G Under Standard Conditions0:17
- Calculating ∆G Under Physiological Conditions2:05
- ∆G < 05:39
- ∆G = 07:03
- Reaction Moving Forward Spontaneously8:00
- ∆G & The Maximum Theoretical Amount of Free Energy Available10:36
- Example Problem 113:11
- Reactions That Have Species in Common17:48
- Example Problem 2: Part 120:10
- Example Problem 2: Part 2- Enzyme Hexokinase & Coupling25:08
- Example Problem 2: Part 330:34
- Recap34:45
ATP & Other High-Energy Compounds
44m 32s
- Intro0:00
- ATP & Other High-Energy Compounds0:10
- Endergonic Reaction Coupled With Exergonic Reaction0:11
- Major Theme In Metabolism6:56
- Why the ∆G°' for ATP Hydrolysis is Large & Negative12:24
- ∆G°' for ATP Hydrolysis12:25
- Reason 1: Electrostatic Repulsion14:24
- Reason 2: Pi & Resonance Forms15:33
- Reason 3: Concentrations of ADP & Pi17:32
- ATP & Other High-Energy Compounds Cont'd18:48
- More On ∆G°' & Hydrolysis18:49
- Other Compounds That Have Large Negative ∆G°' of Hydrolysis: Phosphoenol Pyruvate (PEP)25:14
- Enzyme Pyruvate Kinase30:36
- Another High Energy Molecule: 1,3 Biphosphoglycerate36:17
- Another High Energy Molecule: Phophocreatine39:41
Phosphoryl Group Transfers
30m 8s
- Intro0:00
- Phosphoryl Group Transfer0:27
- Phosphoryl Group Transfer Overview0:28
- Example: Glutamate → Glutamine Part 17:11
- Example: Glutamate → Glutamine Part 213:29
- ATP Not Only Transfers Phosphoryl, But Also Pyrophosphoryl & Adenylyl Groups17:03
- Attack At The γ Phosphorous Transfers a Phosphoryl19:02
- Attack At The β Phosphorous Gives Pyrophosphoryl22:44
Oxidation-Reduction Reactions
49m 46s
- Intro0:00
- Oxidation-Reduction Reactions1:32
- Redox Reactions1:33
- Example 1: Mg + Al³⁺ → Mg²⁺ + Al3:49
- Reduction Potential Definition10:47
- Reduction Potential Example13:38
- Organic Example22:23
- Review: How To Find The Oxidation States For Carbon24:15
- Examples: Oxidation States For Carbon27:45
- Example 1: Oxidation States For Carbon27:46
- Example 2: Oxidation States For Carbon28:36
- Example 3: Oxidation States For Carbon29:18
- Example 4: Oxidation States For Carbon29:44
- Example 5: Oxidation States For Carbon30:10
- Example 6: Oxidation States For Carbon30:40
- Example 7: Oxidation States For Carbon31:20
- Example 8: Oxidation States For Carbon32:10
- Example 9: Oxidation States For Carbon32:52
- Oxidation-Reduction Reactions, cont'd35:22
- More On Reduction Potential35:28
- Lets' Start With ∆G = ∆G°' + RTlnQ38:29
- Example: Oxidation Reduction Reactions41:42
More On Oxidation-Reduction Reactions
56m 34s
- Intro0:00
- More On Oxidation-Reduction Reactions0:10
- Example 1: What If the Concentrations Are Not Standard?0:11
- Alternate Procedure That Uses The 1/2 Reactions Individually8:57
- Universal Electron Carriers in Aqueous Medium: NAD+ & NADH15:12
- The Others Are…19:22
- NAD+ & NADP Coenzymes20:56
- FMN & FAD22:03
- Nicotinamide Adenine Dinucleotide (Phosphate)23:03
- Reduction 1/2 Reactions36:10
- Ratio of NAD+ : NADH36:52
- Ratio of NADPH : NADP+38:02
- Specialized Roles of NAD+ & NADPH38:48
- Oxidoreductase Enzyme Overview40:26
- Examples of Oxidoreductase43:32
- The Flavin Nucleotides46:46
Example Problems For Bioenergetics
42m 12s
- Intro0:00
- Example 1: Calculate the ∆G°' For The Following Reaction1:04
- Example 1: Question1:05
- Example 1: Solution2:20
- Example 2: Calculate the Keq For the Following4:20
- Example 2: Question4:21
- Example 2: Solution5:54
- Example 3: Calculate the ∆G°' For The Hydrolysis of ATP At 25°C8:52
- Example 3: Question8:53
- Example 3: Solution10:30
- Example 3: Alternate Procedure13:48
- Example 4: Problems For Bioenergetics16:46
- Example 4: Questions16:47
- Example 4: Part A Solution21:19
- Example 4: Part B Solution23:26
- Example 4: Part C Solution26:12
- Example 5: Problems For Bioenergetics29:27
- Example 5: Questions29:35
- Example 5: Solution - Part 132:16
- Example 5: Solution - Part 234:39
Section 9: Glycolysis and Gluconeogenesis
Overview of Glycolysis I
43m 32s
- Intro0:00
- Overview of Glycolysis0:48
- Three Primary Paths For Glucose1:04
- Preparatory Phase of Glycolysis4:40
- Payoff Phase of Glycolysis6:40
- Glycolysis Reactions Diagram7:58
- Enzymes of Glycolysis12:41
- Glycolysis Reactions16:02
- Step 116:03
- Step 218:03
- Step 318:52
- Step 420:08
- Step 521:42
- Step 622:44
- Step 724:22
- Step 825:11
- Step 926:00
- Step 1026:51
- Overview of Glycolysis Cont.27:28
- The Overall Reaction for Glycolysis27:29
- Recall The High-Energy Phosphorylated Compounds Discusses In The Bioenergetics Unit33:10
- What Happens To The Pyruvate That Is Formed?37:58
Glycolysis II
1h 1m 47s
- Intro0:00
- Glycolysis Step 1: The Phosphorylation of Glucose0:27
- Glycolysis Step 1: Reaction0:28
- Hexokinase2:28
- Glycolysis Step 1: Mechanism-Simple Nucleophilic Substitution6:34
- Glycolysis Step 2: Conversion of Glucose 6-Phosphate → Fructose 6-Phosphate11:33
- Glycolysis Step 2: Reaction11:34
- Glycolysis Step 2: Mechanism, Part 114:40
- Glycolysis Step 2: Mechanism, Part 218:16
- Glycolysis Step 2: Mechanism, Part 319:56
- Glycolysis Step 2: Mechanism, Part 4 (Ring Closing & Dissociation)21:54
- Glycolysis Step 3: Conversion of Fructose 6-Phosphate to Fructose 1,6-Biphosphate24:16
- Glycolysis Step 3: Reaction24:17
- Glycolysis Step 3: Mechanism26:40
- Glycolysis Step 4: Cleavage of Fructose 1,6-Biphosphate31:10
- Glycolysis Step 4: Reaction31:11
- Glycolysis Step 4: Mechanism, Part 1 (Binding & Ring Opening)35:26
- Glycolysis Step 4: Mechanism, Part 237:40
- Glycolysis Step 4: Mechanism, Part 339:30
- Glycolysis Step 4: Mechanism, Part 444:00
- Glycolysis Step 4: Mechanism, Part 546:34
- Glycolysis Step 4: Mechanism, Part 649:00
- Glycolysis Step 4: Mechanism, Part 750:12
- Hydrolysis of The Imine52:33
- Glycolysis Step 5: Conversion of Dihydroxyaceton Phosphate to Glyceraldehyde 3-Phosphate55:38
- Glycolysis Step 5: Reaction55:39
- Breakdown and Numbering of Sugar57:40
Glycolysis III
59m 17s
- Intro0:00
- Glycolysis Step 5: Conversion of Dihydroxyaceton Phosphate to Glyceraldehyde 3-Phosphate0:44
- Glycolysis Step 5: Mechanism, Part 10:45
- Glycolysis Step 5: Mechanism, Part 23:53
- Glycolysis Step 6: Oxidation of Glyceraldehyde 3-Phosphate to 1,3-Biphosphoglycerate5:14
- Glycolysis Step 6: Reaction5:15
- Glycolysis Step 6: Mechanism, Part 18:52
- Glycolysis Step 6: Mechanism, Part 212:58
- Glycolysis Step 6: Mechanism, Part 314:26
- Glycolysis Step 6: Mechanism, Part 416:23
- Glycolysis Step 7: Phosphoryl Transfer From 1,3-Biphosphoglycerate to ADP to Form ATP19:08
- Glycolysis Step 7: Reaction19:09
- Substrate-Level Phosphorylation23:18
- Glycolysis Step 7: Mechanism (Nucleophilic Substitution)26:57
- Glycolysis Step 8: Conversion of 3-Phosphoglycerate to 2-Phosphoglycerate28:44
- Glycolysis Step 8: Reaction28:45
- Glycolysis Step 8: Mechanism, Part 130:08
- Glycolysis Step 8: Mechanism, Part 232:24
- Glycolysis Step 8: Mechanism, Part 334:02
- Catalytic Cycle35:42
- Glycolysis Step 9: Dehydration of 2-Phosphoglycerate to Phosphoenol Pyruvate37:20
- Glycolysis Step 9: Reaction37:21
- Glycolysis Step 9: Mechanism, Part 140:12
- Glycolysis Step 9: Mechanism, Part 242:01
- Glycolysis Step 9: Mechanism, Part 343:58
- Glycolysis Step 10: Transfer of a Phosphoryl Group From Phosphoenol Pyruvate To ADP To Form ATP45:16
- Glycolysis Step 10: Reaction45:17
- Substrate-Level Phosphorylation48:32
- Energy Coupling Reaction51:24
- Glycolysis Balance Sheet54:15
- Glycolysis Balance Sheet54:16
- What Happens to The 6 Carbons of Glucose?56:22
- What Happens to 2 ADP & 2 Pi?57:04
- What Happens to The 4e⁻ ?57:15
Glycolysis IV
39m 47s
- Intro0:00
- Feeder Pathways0:42
- Feeder Pathways Overview0:43
- Starch, Glycogen2:25
- Lactose4:38
- Galactose4:58
- Manose5:22
- Trehalose5:45
- Sucrose5:56
- Fructose6:07
- Fates of Pyruvate: Aerobic & Anaerobic Conditions7:39
- Aerobic Conditions & Pyruvate7:40
- Anaerobic Fates of Pyruvate11:18
- Fates of Pyruvate: Lactate Acid Fermentation14:10
- Lactate Acid Fermentation14:11
- Fates of Pyruvate: Ethanol Fermentation19:01
- Ethanol Fermentation Reaction19:02
- TPP: Thiamine Pyrophosphate (Functions and Structure)23:10
- Ethanol Fermentation Mechanism, Part 127:53
- Ethanol Fermentation Mechanism, Part 229:06
- Ethanol Fermentation Mechanism, Part 331:15
- Ethanol Fermentation Mechanism, Part 432:44
- Ethanol Fermentation Mechanism, Part 534:33
- Ethanol Fermentation Mechanism, Part 635:48
Gluconeogenesis I
41m 34s
- Intro0:00
- Gluconeogenesis, Part 11:02
- Gluconeogenesis Overview1:03
- 3 Glycolytic Reactions That Are Irreversible Under Physiological Conditions2:29
- Gluconeogenesis Reactions Overview6:17
- Reaction: Pyruvate to Oxaloacetate11:07
- Reaction: Oxaloacetate to Phosphoenolpyruvate (PEP)13:29
- First Pathway That Pyruvate Can Take to Become Phosphoenolpyruvate15:24
- Second Pathway That Pyruvate Can Take to Become Phosphoenolpyruvate21:00
- Transportation of Pyruvate From The Cytosol to The Mitochondria24:15
- Transportation Mechanism, Part 126:41
- Transportation Mechanism, Part 230:43
- Transportation Mechanism, Part 334:04
- Transportation Mechanism, Part 438:14
Gluconeogenesis II
34m 18s
- Intro0:00
- Oxaloacetate → Phosphoenolpyruvate (PEP)0:35
- Mitochondrial Membrane Does Not Have a Transporter for Oxaloactate0:36
- Reaction: Oxaloacetate to Phosphoenolpyruvate (PEP)3:36
- Mechanism: Oxaloacetate to Phosphoenolpyruvate (PEP)4:48
- Overall Reaction: Pyruvate to Phosphoenolpyruvate7:01
- Recall The Two Pathways That Pyruvate Can Take to Become Phosphoenolpyruvate10:16
- NADH in Gluconeogenesis12:29
- Second Pathway: Lactate → Pyruvate18:22
- Cytosolic PEP Carboxykinase, Mitochondrial PEP Carboxykinase, & Isozymes18:23
- 2nd Bypass Reaction23:04
- 3rd Bypass Reaction24:01
- Overall Process25:17
- Other Feeder Pathways For Gluconeogenesis26:35
- Carbon Intermediates of The Citric Acid Cycle26:36
- Amino Acids & The Gluconeogenic Pathway29:45
- Glycolysis & Gluconeogenesis Are Reciprocally Regulated32:00
The Pentose Phosphate Pathway
42m 52s
- Intro0:00
- The Pentose Phosphate Pathway Overview0:17
- The Major Fate of Glucose-6-Phosphate0:18
- The Pentose Phosphate Pathway (PPP) Overview1:00
- Oxidative Phase of The Pentose Phosphate Pathway4:33
- Oxidative Phase of The Pentose Phosphate Pathway: Reaction Overview4:34
- Ribose-5-Phosphate: Glutathione & Reductive Biosynthesis9:02
- Glucose-6-Phosphate to 6-Phosphogluconate12:48
- 6-Phosphogluconate to Ribulose-5-Phosphate15:39
- Ribulose-5-Phosphate to Ribose-5-Phosphate17:05
- Non-Oxidative Phase of The Pentose Phosphate Pathway19:55
- Non-Oxidative Phase of The Pentose Phosphate Pathway: Overview19:56
- General Transketolase Reaction29:03
- Transaldolase Reaction35:10
- Final Transketolase Reaction39:10
Section 10: The Citric Acid Cycle (Krebs Cycle)
Citric Acid Cycle I
36m 10s
- Intro0:00
- Stages of Cellular Respiration0:23
- Stages of Cellular Respiration0:24
- From Pyruvate to Acetyl-CoA6:56
- From Pyruvate to Acetyl-CoA: Pyruvate Dehydrogenase Complex6:57
- Overall Reaction8:42
- Oxidative Decarboxylation11:54
- Pyruvate Dehydrogenase (PDH) & Enzymes15:30
- Pyruvate Dehydrogenase (PDH) Requires 5 Coenzymes17:15
- Molecule of CoEnzyme A18:52
- Thioesters20:56
- Lipoic Acid22:31
- Lipoate Is Attached To a Lysine Residue On E₂24:42
- Pyruvate Dehydrogenase Complex: Reactions26:36
- E1: Reaction 1 & 230:38
- E2: Reaction 331:58
- E3: Reaction 4 & 532:44
- Substrate Channeling34:17
Citric Acid Cycle II
49m 20s
- Intro0:00
- Citric Acid Cycle Reactions Overview0:26
- Citric Acid Cycle Reactions Overview: Part 10:27
- Citric Acid Cycle Reactions Overview: Part 27:03
- Things to Note10:58
- Citric Acid Cycle Reactions & Mechanism13:57
- Reaction 1: Formation of Citrate13:58
- Reaction 1: Mechanism19:01
- Reaction 2: Citrate to Cis Aconistate to Isocitrate28:50
- Reaction 3: Isocitrate to α-Ketoglutarate32:35
- Reaction 3: Two Isocitrate Dehydrogenase Enzymes36:24
- Reaction 3: Mechanism37:33
- Reaction 4: Oxidation of α-Ketoglutarate to Succinyl-CoA41:38
- Reaction 4: Notes46:34
Citric Acid Cycle III
44m 11s
- Intro0:00
- Citric Acid Cycle Reactions & Mechanism0:21
- Reaction 5: Succinyl-CoA to Succinate0:24
- Reaction 5: Reaction Sequence2:35
- Reaction 6: Oxidation of Succinate to Fumarate8:28
- Reaction 7: Fumarate to Malate10:17
- Reaction 8: Oxidation of L-Malate to Oxaloacetate14:15
- More On The Citric Acid Cycle17:17
- Energy from Oxidation17:18
- How Can We Transfer This NADH Into the Mitochondria27:10
- Citric Cycle is Amphibolic - Works In Both Anabolic & Catabolic Pathways32:06
- Biosynthetic Processes34:29
- Anaplerotic Reactions Overview37:26
- Anaplerotic: Reaction 141:42
Section 11: Catabolism of Fatty Acids
Fatty Acid Catabolism I
48m 11s
- Intro0:00
- Introduction to Fatty Acid Catabolism0:21
- Introduction to Fatty Acid Catabolism0:22
- Vertebrate Cells Obtain Fatty Acids for Catabolism From 3 Sources2:16
- Diet: Part 14:00
- Diet: Part 25:35
- Diet: Part 36:20
- Diet: Part 46:47
- Diet: Part 510:18
- Diet: Part 610:54
- Diet: Part 712:04
- Diet: Part 812:26
- Fats Stored in Adipocytes Overview13:54
- Fats Stored in Adipocytes (Fat Cells): Part 116:13
- Fats Stored in Adipocytes (Fat Cells): Part 217:16
- Fats Stored in Adipocytes (Fat Cells): Part 319:42
- Fats Stored in Adipocytes (Fat Cells): Part 420:52
- Fats Stored in Adipocytes (Fat Cells): Part 522:56
- Mobilization of TAGs Stored in Fat Cells24:35
- Fatty Acid Oxidation28:29
- Fatty Acid Oxidation28:48
- 3 Reactions of the Carnitine Shuttle30:42
- Carnitine Shuttle & The Mitochondrial Matrix36:25
- CAT I43:58
- Carnitine Shuttle is the Rate-Limiting Steps46:24
Fatty Acid Catabolism II
45m 58s
- Intro0:00
- Fatty Acid Catabolism0:15
- Fatty Acid Oxidation Takes Place in 3 Stages0:16
- β-Oxidation2:05
- β-Oxidation Overview2:06
- Reaction 14:20
- Reaction 27:35
- Reaction 38:52
- Reaction 410:16
- β-Oxidation Reactions Discussion11:34
- Notes On β-Oxidation15:14
- Double Bond After The First Reaction15:15
- Reaction 1 is Catalyzed by 3 Isozymes of Acyl-CoA Dehydrogenase16:04
- Reaction 2 & The Addition of H₂O18:38
- After Reaction 419:24
- Production of ATP20:04
- β-Oxidation of Unsaturated Fatty Acid21:25
- β-Oxidation of Unsaturated Fatty Acid22:36
- β-Oxidation of Mono-Unsaturates24:49
- β-Oxidation of Mono-Unsaturates: Reaction 124:50
- β-Oxidation of Mono-Unsaturates: Reaction 228:43
- β-Oxidation of Mono-Unsaturates: Reaction 330:50
- β-Oxidation of Mono-Unsaturates: Reaction 431:06
- β-Oxidation of Polyunsaturates32:29
- β-Oxidation of Polyunsaturates: Part 132:30
- β-Oxidation of Polyunsaturates: Part 237:08
- β-Oxidation of Polyunsaturates: Part 340:25
Fatty Acid Catabolism III
33m 18s
- Intro0:00
- Fatty Acid Catabolism0:43
- Oxidation of Fatty Acids With an Odd Number of Carbons0:44
- β-oxidation in the Mitochondrion & Two Other Pathways9:08
- ω-oxidation10:37
- α-oxidation17:22
- Ketone Bodies19:08
- Two Fates of Acetyl-CoA Formed by β-Oxidation Overview19:09
- Ketone Bodies: Acetone20:42
- Ketone Bodies: Acetoacetate20:57
- Ketone Bodies: D-β-hydroxybutyrate21:25
- Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 122:05
- Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 226:59
- Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 330:52
Section 12: Catabolism of Amino Acids and the Urea Cycle
Overview & The Aminotransferase Reaction
40m 59s
- Intro0:00
- Overview of The Aminotransferase Reaction0:25
- Overview of The Aminotransferase Reaction0:26
- The Aminotransferase Reaction: Process 13:06
- The Aminotransferase Reaction: Process 26:46
- Alanine From Muscle Tissue10:54
- Bigger Picture of the Aminotransferase Reaction14:52
- Looking Closely at Process 119:04
- Pyridoxal Phosphate (PLP)24:32
- Pyridoxamine Phosphate25:29
- Pyridoxine (B6)26:38
- The Function of PLP27:12
- Mechanism Examples28:46
- Reverse Reaction: Glutamate to α-Ketoglutarate35:34
Glutamine & Alanine: The Urea Cycle I
39m 18s
- Intro0:00
- Glutamine & Alanine: The Urea Cycle I0:45
- Excess Ammonia, Glutamate, and Glutamine0:46
- Glucose-Alanine Cycle9:54
- Introduction to the Urea Cycle20:56
- The Urea Cycle: Production of the Carbamoyl Phosphate22:59
- The Urea Cycle: Reaction & Mechanism Involving the Carbamoyl Phosphate Synthetase33:36
Glutamine & Alanine: The Urea Cycle II
36m 21s
- Intro0:00
- Glutamine & Alanine: The Urea Cycle II0:14
- The Urea Cycle Overview0:34
- Reaction 1: Ornithine → Citrulline7:30
- Reaction 2: Citrulline → Citrullyl-AMP11:15
- Reaction 2': Citrullyl-AMP → Argininosuccinate15:25
- Reaction 3: Argininosuccinate → Arginine20:42
- Reaction 4: Arginine → Orthinine24:00
- Links Between the Citric Acid Cycle & the Urea Cycle27:47
- Aspartate-argininosuccinate Shunt32:36
Amino Acid Catabolism
47m 58s
- Intro0:00
- Amino Acid Catabolism0:10
- Common Amino Acids and 6 Major Products0:11
- Ketogenic Amino Acid1:52
- Glucogenic Amino Acid2:51
- Amino Acid Catabolism Diagram4:18
- Cofactors That Play a Role in Amino Acid Catabolism7:00
- Biotin8:42
- Tetrahydrofolate10:44
- S-Adenosylmethionine (AdoMet)12:46
- Tetrahydrobiopterin13:53
- S-Adenosylmethionine & Tetrahydrobiopterin Molecules14:41
- Catabolism of Phenylalanine18:30
- Reaction 1: Phenylalanine to Tyrosine18:31
- Reaction 2: Tyrosine to p-Hydroxyphenylpyruvate21:36
- Reaction 3: p-Hydroxyphenylpyruvate to Homogentisate23:50
- Reaction 4: Homogentisate to Maleylacetoacetate25:42
- Reaction 5: Maleylacetoacetate to Fumarylacetoacetate28:20
- Reaction 6: Fumarylacetoacetate to Fumarate & Succinyl-CoA29:51
- Reaction 7: Fate of Fumarate & Succinyl-CoA31:14
- Phenylalanine Hydroxylase33:33
- The Phenylalanine Hydroxylase Reaction33:34
- Mixed-Function Oxidases40:26
- When Phenylalanine Hydoxylase is Defective: Phenylketonuria (PKU)44:13
Section 13: Oxidative Phosphorylation and ATP Synthesis
Oxidative Phosphorylation I
41m 11s
- Intro0:00
- Oxidative Phosphorylation0:54
- Oxidative Phosphorylation Overview0:55
- Mitochondrial Electron Transport Chain Diagram7:15
- Enzyme Complex I of the Electron Transport Chain12:27
- Enzyme Complex II of the Electron Transport Chain14:02
- Enzyme Complex III of the Electron Transport Chain14:34
- Enzyme Complex IV of the Electron Transport Chain15:30
- Complexes Diagram16:25
- Complex I18:25
- Complex I Overview18:26
- What is Ubiquinone or Coenzyme Q?20:02
- Coenzyme Q Transformation22:37
- Complex I Diagram24:47
- Fe-S Proteins26:42
- Transfer of H⁺29:42
- Complex II31:06
- Succinate Dehydrogenase31:07
- Complex II Diagram & Process32:54
- Other Substrates Pass Their e⁻ to Q: Glycerol 3-Phosphate37:31
- Other Substrates Pass Their e⁻ to Q: Fatty Acyl-CoA39:02
Oxidative Phosphorylation II
36m 27s
- Intro0:00
- Complex III0:19
- Complex III Overview0:20
- Complex III: Step 11:56
- Complex III: Step 26:14
- Complex IV8:42
- Complex IV: Cytochrome Oxidase8:43
- Oxidative Phosphorylation, cont'd17:18
- Oxidative Phosphorylation: Summary17:19
- Equation 119:13
- How Exergonic is the Reaction?21:03
- Potential Energy Represented by Transported H⁺27:24
- Free Energy Change for the Production of an Electrochemical Gradient Via an Ion Pump28:48
- Free Energy Change in Active Mitochondria32:02
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