Section 1: Preliminaries on Aqueous Chemistry |
|
Aqueous Solutions & Concentration |
39:57 |
| |
Intro |
0:00 | |
| |
Aqueous Solutions and Concentration |
0:46 | |
| |
| Definition of Solution |
1:28 | |
| |
| Example: Sugar Dissolved in Water |
2:19 | |
| |
| Example: Salt Dissolved in Water |
3:04 | |
| |
| A Solute Does Not Have to Be a Solid |
3:37 | |
| |
| A Solvent Does Not Have to Be a Liquid |
5:02 | |
| |
| Covalent Compounds |
6:55 | |
| |
| Ionic Compounds |
7:39 | |
| |
| Example: Table Sugar |
9:12 | |
| |
| Example: MgCl₂ |
10:40 | |
| |
| Expressing Concentration: Molarity |
13:42 | |
| |
Example 1 |
14:47 | |
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| Example 1: Question |
14:50 | |
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| Example 1: Solution |
15:40 | |
| |
| Another Way to Express Concentration |
22:01 | |
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Example 2 |
24:00 | |
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| Example 2: Question |
24:01 | |
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| Example 2: Solution |
24:49 | |
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| Some Other Ways of Expressing Concentration |
27:52 | |
| |
Example 3 |
29:30 | |
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| Example 3: Question |
29:31 | |
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| Example 3: Solution |
31:02 | |
|
Dilution & Osmotic Pressure |
38:53 |
| |
Intro |
0:00 | |
| |
Dilution |
0:45 | |
| |
| Definition of Dilution |
0:46 | |
| |
| Example 1: Question |
2:08 | |
| |
| Example 1: Basic Dilution Equation |
4:20 | |
| |
| Example 1: Solution |
5:31 | |
| |
| Example 2: Alternative Approach |
12:05 | |
| |
Osmotic Pressure |
14:34 | |
| |
| Colligative Properties |
15:02 | |
| |
| Recall: Covalent Compounds and Soluble Ionic Compounds |
17:24 | |
| |
| Properties of Pure Water |
19:42 | |
| |
| Addition of a Solute |
21:56 | |
| |
| Osmotic Pressure: Conceptual Example |
24:00 | |
| |
| Equation for Osmotic Pressure |
29:30 | |
| |
| Example of 'i' |
31:38 | |
| |
| Example 3 |
32:50 | |
|
More on Osmosis |
29:01 |
| |
Intro |
0:00 | |
| |
More on Osmosis |
1:25 | |
| |
| Osmotic Pressure |
1:26 | |
| |
| Example 1: Molar Mass of Protein |
5:25 | |
| |
| Definition, Equation, and Unit of Osmolarity |
13:13 | |
| |
| Example 2: Osmolarity |
15:19 | |
| |
| Isotonic, Hypertonic, and Hypotonic |
20:20 | |
| |
| Example 3 |
22:20 | |
| |
| More on Isotonic, Hypertonic, and Hypotonic |
26:14 | |
| |
| Osmosis vs. Osmotic Pressure |
27:56 | |
|
Acids & Bases |
39:11 |
| |
Intro |
0:00 | |
| |
Acids and Bases |
1:16 | |
| |
| Let's Begin With H₂O |
1:17 | |
| |
| P-Scale |
4:22 | |
| |
| Example 1 |
6:39 | |
| |
| pH |
9:43 | |
| |
| Strong Acids |
11:10 | |
| |
| Strong Bases |
13:52 | |
| |
| Weak Acids & Bases Overview |
14:32 | |
| |
| Weak Acids |
15:49 | |
| |
| Example 2: Phosphoric Acid |
19:30 | |
| |
| Weak Bases |
24:50 | |
| |
| Weak Base Produces Hydroxide Indirectly |
25:41 | |
| |
| Example 3: Pyridine |
29:07 | |
| |
| Acid Form and Base Form |
32:02 | |
| |
| Acid Reaction |
35:50 | |
| |
| Base Reaction |
36:27 | |
| |
| Ka, Kb, and Kw |
37:14 | |
|
Titrations and Buffers |
41:33 |
| |
Intro |
0:00 | |
| |
Titrations |
0:27 | |
| |
| Weak Acid |
0:28 | |
| |
| Rearranging the Ka Equation |
1:45 | |
| |
| Henderson-Hasselbalch Equation |
3:52 | |
| |
| Fundamental Reaction of Acids and Bases |
5:36 | |
| |
| The Idea Behind a Titration |
6:27 | |
| |
| Let's Look at an Acetic Acid Solution |
8:44 | |
| |
| Titration Curve |
17:00 | |
| |
| Acetate |
23:57 | |
| |
Buffers |
26:57 | |
| |
| Introduction to Buffers |
26:58 | |
| |
| What is a Buffer? |
29:40 | |
| |
| Titration Curve & Buffer Region |
31:44 | |
| |
| How a Buffer Works: Adding OH⁻ |
34:44 | |
| |
| How a Buffer Works: Adding H⁺ |
35:58 | |
| |
| Phosphate Buffer System |
38:02 | |
|
Example Problems with Acids, Bases & Buffers |
44:19 |
| |
Intro |
0:00 | |
| |
Example 1 |
1:21 | |
| |
| Example 1: Properties of Glycine |
1:22 | |
| |
| Example 1: Part A |
3:40 | |
| |
| Example 1: Part B |
4:40 | |
| |
Example 2 |
9:02 | |
| |
| Example 2: Question |
9:03 | |
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| Example 2: Total Phosphate Concentration |
12:23 | |
| |
| Example 2: Final Solution |
17:10 | |
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Example 3 |
19:34 | |
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| Example 3: Question |
19:35 | |
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| Example 3: pH Before |
22:18 | |
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| Example 3: pH After |
24:24 | |
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| Example 3: New pH |
27:54 | |
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Example 4 |
30:00 | |
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| Example 4: Question |
30:01 | |
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| Example 4: Equilibria |
32:52 | |
| |
| Example 4: 1st Reaction |
38:04 | |
| |
| Example 4: 2nd Reaction |
39:53 | |
| |
| Example 4: Final Solution |
41:33 | |
|
Hydrolysis & Condensation Reactions |
18:45 |
| |
Intro |
0:00 | |
| |
Hydrolysis and Condensation Reactions |
0:50 | |
| |
| Hydrolysis |
0:51 | |
| |
| Condensation |
2:42 | |
| |
| Example 1: Hydrolysis of Ethyl Acetate |
4:52 | |
| |
| Example 2: Condensation of Acetic Acid with Ethanol |
8:42 | |
| |
| Example 3 |
11:18 | |
| |
| Example 4: Formation & Hydrolysis of a Peptide Bond Between the Amino Acids Alanine & Serine |
14:56 | |
Section 2: Amino Acids & Proteins: Primary Structure |
|
Amino Acids |
38:19 |
| |
Intro |
0:00 | |
| |
Amino Acids |
0:17 | |
| |
| Proteins & Amino Acids |
0:18 | |
| |
| Difference Between Amino Acids |
4:20 | |
| |
| α-Carbon |
7:08 | |
| |
| Configuration in Biochemistry |
10:43 | |
| |
| L-Glyceraldehyde & Fischer Projection |
12:32 | |
| |
| D-Glyceraldehyde & Fischer Projection |
15:31 | |
| |
| Amino Acids in Biological Proteins are the L Enantiomer |
16:50 | |
| |
| L-Amino Acid |
18:04 | |
| |
| L-Amino Acids Correspond to S-Enantiomers in the RS System |
20:10 | |
| |
| Classification of Amino Acids |
22:53 | |
| |
Amino Acids With Non-Polar R Groups |
26:45 | |
| |
| Glycine |
27:00 | |
| |
| Alanine |
27:48 | |
| |
| Valine |
28:15 | |
| |
| Leucine |
28:58 | |
| |
| Proline |
31:08 | |
| |
| Isoleucine |
32:42 | |
| |
| Methionine |
33:43 | |
| |
Amino Acids With Aromatic R Groups |
34:33 | |
| |
| Phenylalanine |
35:26 | |
| |
| Tyrosine |
36:02 | |
| |
| Tryptophan |
36:32 | |
|
Amino Acids, Continued |
27:14 |
| |
Intro |
0:00 | |
| |
Amino Acids With Positively Charged R Groups |
0:16 | |
| |
| Lysine |
0:52 | |
| |
| Arginine |
1:55 | |
| |
| Histidine |
3:15 | |
| |
Amino Acids With Negatively Charged R Groups |
6:28 | |
| |
| Aspartate |
6:58 | |
| |
| Glutamate |
8:11 | |
| |
Amino Acids With Uncharged, but Polar R Groups |
8:50 | |
| |
| Serine |
8:51 | |
| |
| Threonine |
10:21 | |
| |
| Cysteine |
11:06 | |
| |
| Asparagine |
11:35 | |
| |
| Glutamine |
12:44 | |
| |
More on Amino Acids |
14:18 | |
| |
| Cysteine Dimerizes to Form Cystine |
14:53 | |
| |
| Tryptophan, Tyrosine, and Phenylalanine |
19:07 | |
| |
| Other Amino Acids |
20:53 | |
| |
| Other Amino Acids: Hydroxy Lysine |
22:34 | |
| |
| Other Amino Acids: r-Carboxy Glutamate |
25:37 | |
|
Acid/Base Behavior of Amino Acids |
48:28 |
| |
Intro |
0:00 | |
| |
Acid/Base Behavior of Amino Acids |
0:27 | |
| |
| Acid/Base Behavior of Amino Acids |
0:28 | |
| |
| Let's Look at Alanine |
1:57 | |
| |
| Titration of Acidic Solution of Alanine with a Strong Base |
2:51 | |
| |
| Amphoteric Amino Acids |
13:24 | |
| |
| Zwitterion & Isoelectric Point |
16:42 | |
| |
| Some Amino Acids Have 3 Ionizable Groups |
20:35 | |
| |
| Example: Aspartate |
24:44 | |
| |
| Example: Tyrosine |
28:50 | |
| |
| Rule of Thumb |
33:04 | |
| |
| Basis for the Rule |
35:59 | |
| |
| Example: Describe the Degree of Protonation for Each Ionizable Group |
38:46 | |
| |
| Histidine is Special |
44:58 | |
|
Peptides & Proteins |
45:18 |
| |
Intro |
0:00 | |
| |
Peptides and Proteins |
0:15 | |
| |
| Introduction to Peptides and Proteins |
0:16 | |
| |
| Formation of a Peptide Bond: The Bond Between 2 Amino Acids |
1:44 | |
| |
| Equilibrium |
7:53 | |
| |
| Example 1: Build the Following Tripeptide Ala-Tyr-Ile |
9:48 | |
| |
| Example 1: Shape Structure |
15:43 | |
| |
| Example 1: Line Structure |
17:11 | |
| |
| Peptides Bonds |
20:08 | |
| |
| Terms We'll Be Using Interchangeably |
23:14 | |
| |
| Biological Activity & Size of a Peptide |
24:58 | |
| |
| Multi-Subunit Proteins |
30:08 | |
| |
| Proteins and Prosthetic Groups |
32:13 | |
| |
| Carbonic Anhydrase |
37:35 | |
| |
| Primary, Secondary, Tertiary, and Quaternary Structure of Proteins |
40:26 | |
|
Amino Acid Sequencing of a Peptide Chain |
42:47 |
| |
Intro |
0:00 | |
| |
Amino Acid Sequencing of a Peptide Chain |
0:30 | |
| |
| Amino Acid Sequence and Its Structure |
0:31 | |
| |
| Edman Degradation: Overview |
2:57 | |
| |
| Edman Degradation: Reaction - Part 1 |
4:58 | |
| |
| Edman Degradation: Reaction - Part 2 |
10:28 | |
| |
| Edman Degradation: Reaction - Part 3 |
13:51 | |
| |
| Mechanism Step 1: PTC (Phenylthiocarbamyl) Formation |
19:01 | |
| |
| Mechanism Step 2: Ring Formation & Peptide Bond Cleavage |
23:03 | |
| |
Example: Write Out the Edman Degradation for the Tripeptide Ala-Tyr-Ser |
30:29 | |
| |
| Step 1 |
30:30 | |
| |
| Step 2 |
34:21 | |
| |
| Step 3 |
36:56 | |
| |
| Step 4 |
38:28 | |
| |
| Step 5 |
39:24 | |
| |
| Step 6 |
40:44 | |
|
Sequencing Larger Peptides & Proteins |
1:02:33 |
| |
Intro |
0:00 | |
| |
Sequencing Larger Peptides and Proteins |
0:28 | |
| |
| Identifying the N-Terminal Amino Acids With the Reagent Fluorodinitrobenzene (FDNB) |
0:29 | |
| |
| Sequencing Longer Peptides & Proteins Overview |
5:54 | |
| |
| Breaking Peptide Bond: Proteases and Chemicals |
8:16 | |
| |
| Some Enzymes/Chemicals Used for Fragmentation: Trypsin |
11:14 | |
| |
| Some Enzymes/Chemicals Used for Fragmentation: Chymotrypsin |
13:02 | |
| |
| Some Enzymes/Chemicals Used for Fragmentation: Cyanogen Bromide |
13:28 | |
| |
| Some Enzymes/Chemicals Used for Fragmentation: Pepsin |
13:44 | |
| |
| Cleavage Location |
14:04 | |
| |
| Example: Chymotrypsin |
16:44 | |
| |
| Example: Pepsin |
18:17 | |
| |
| More on Sequencing Larger Peptides and Proteins |
19:29 | |
| |
| Breaking Disulfide Bonds: Performic Acid |
26:08 | |
| |
| Breaking Disulfide Bonds: Dithiothreitol Followed by Iodoacetate |
31:04 | |
| |
Example: Sequencing Larger Peptides and Proteins |
37:03 | |
| |
| Part 1 - Breaking Disulfide Bonds, Hydrolysis and Separation |
37:04 | |
| |
| Part 2 - N-Terminal Identification |
44:16 | |
| |
| Part 3 - Sequencing Using Pepsin |
46:43 | |
| |
| Part 4 - Sequencing Using Cyanogen Bromide |
52:02 | |
| |
| Part 5 - Final Sequence |
56:48 | |
|
Peptide Synthesis (Merrifield Process) |
49:12 |
| |
Intro |
0:00 | |
| |
Peptide Synthesis (Merrifield Process) |
0:31 | |
| |
| Introduction to Synthesizing Peptides |
0:32 | |
| |
| Merrifield Peptide Synthesis: General Scheme |
3:03 | |
| |
| So What Do We Do? |
6:07 | |
| |
| Synthesis of Protein in the Body Vs. The Merrifield Process |
7:40 | |
| |
Example: Synthesis of Ala-Gly-Ser |
9:21 | |
| |
| Synthesis of Ala-Gly-Ser: Reactions Overview |
11:41 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 1 |
19:34 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 2 |
24:34 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 3 |
27:34 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 4 & 4a |
28:48 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 5 |
33:38 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 6 |
36:45 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 7 & 7a |
37:44 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 8 |
39:47 | |
| |
| Synthesis of Ala-Gly-Ser: Reaction 9 & 10 |
43:23 | |
| |
Chromatography: Eluent, Stationary Phase, and Eluate |
45:55 | |
|
More Examples with Amino Acids & Peptides |
54:31 |
| |
Intro |
0:00 | |
| |
Example 1 |
0:22 | |
| |
| Data |
0:23 | |
| |
| Part A: What is the pI of Serine & Draw the Correct Structure |
2:11 | |
| |
| 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 Serine |
10:50 | |
| |
| Part D: Draw the Titration Curve for This Situation |
14:50 | |
| |
| Part E: The 10 mL of NaOH Added to the Solution at the pI is How Many Equivalents? |
17:35 | |
| |
| Part F: Serine Buffer Solution |
20:22 | |
| |
Example 2 |
23:04 | |
| |
| Data |
23:05 | |
| |
| Part A: Calculate the Minimum Molar Mass of the Protein |
25:12 | |
| |
| Part B: How Many Tyr Residues in this Protein? |
28:34 | |
| |
Example 3 |
30:08 | |
| |
| Question |
30:09 | |
| |
| Solution |
34:30 | |
| |
Example 4 |
48:46 | |
| |
| Question |
48:47 | |
| |
| Solution |
49:50 | |
Section 3: Proteins: Secondary, Tertiary, and Quaternary Structure |
|
Alpha Helix & Beta Conformation |
50:52 |
| |
Intro |
0:00 | |
| |
Alpha Helix and Beta Conformation |
0:28 | |
| |
| Protein Structure Overview |
0:29 | |
| |
| Weak interactions Among the Amino Acid in the Peptide Chain |
2:11 | |
| |
| Two Principals of Folding Patterns |
4:56 | |
| |
| Peptide Bond |
7:00 | |
| |
| Peptide Bond: Resonance |
9:46 | |
| |
| Peptide Bond: φ Bond & ψ Bond |
11:22 | |
| |
| Secondary Structure |
15:08 | |
| |
| α-Helix Folding Pattern |
17:28 | |
| |
| Illustration 1: α-Helix Folding Pattern |
19:22 | |
| |
| Illustration 2: α-Helix Folding Pattern |
21:39 | |
| |
| β-Sheet |
25:16 | |
| |
| β-Conformation |
26:04 | |
| |
| Parallel & Anti-parallel |
28:44 | |
| |
| Parallel β-Conformation Arrangement of the Peptide Chain |
30:12 | |
| |
| Putting Together a Parallel Peptide Chain |
35:16 | |
| |
| Anti-Parallel β-Conformation Arrangement |
37:42 | |
| |
| Tertiary Structure |
45:03 | |
| |
| Quaternary Structure |
45:52 | |
| |
| Illustration 3: Myoglobin Tertiary Structure & Hemoglobin Quaternary Structure |
47:13 | |
| |
| Final Words on Alpha Helix and Beta Conformation |
48:34 | |
Section 4: Proteins: Function |
|
Protein Function I: Ligand Binding & Myoglobin |
51:36 |
| |
Intro |
0:00 | |
| |
Protein Function I: Ligand Binding & Myoglobin |
0:30 | |
| |
| Ligand |
1:02 | |
| |
| Binding Site |
2:06 | |
| |
| Proteins are Not Static or Fixed |
3:36 | |
| |
| Multi-Subunit Proteins |
5:46 | |
| |
| O₂ as a Ligand |
7:21 | |
| |
| Myoglobin, Protoporphyrin IX, Fe ²⁺, and O₂ |
12:54 | |
| |
| Protoporphyrin Illustration |
14:25 | |
| |
| Myoglobin With a Heme Group Illustration |
17:02 | |
| |
| Fe²⁺ has 6 Coordination Sites & Binds O₂ |
18:10 | |
| |
| Heme |
19:44 | |
| |
| Myoglobin Overview |
22:40 | |
| |
| Myoglobin and O₂ Interaction |
23:34 | |
| |
| Keq or Ka & The Measure of Protein's Affinity for Its Ligand |
26:46 | |
| |
| Defining α: Fraction of Binding Sites Occupied |
32:52 | |
| |
| Graph: α vs. [L] |
37:33 | |
| |
| For The Special Case of α = 0.5 |
39:01 | |
| |
| Association Constant & Dissociation Constant |
43:54 | |
| |
| α & Kd |
45:15 | |
| |
| Myoglobin's Binding of O₂ |
48:20 | |
|
Protein Function II: Hemoglobin |
1:03:36 |
| |
Intro |
0:00 | |
| |
Protein Function II: Hemoglobin |
0:14 | |
| |
| Hemoglobin Overview |
0:15 | |
| |
| Hemoglobin & Its 4 Subunits |
1:22 | |
| |
| α and β Interactions |
5:18 | |
| |
| Two Major Conformations of Hb: T State (Tense) & R State (Relaxed) |
8:06 | |
| |
| Transition From The T State to R State |
12:03 | |
| |
| Binding of Hemoglobins & O₂ |
14:02 | |
| |
| Binding Curve |
18:32 | |
| |
| Hemoglobin in the Lung |
27:28 | |
| |
| Signoid Curve |
30:13 | |
| |
| Cooperative Binding |
32:25 | |
| |
| Hemoglobin is an Allosteric Protein |
34:26 | |
| |
| Homotropic Allostery |
36:18 | |
| |
| Describing Cooperative Binding Quantitatively |
38:06 | |
| |
| Deriving The Hill Equation |
41:52 | |
| |
| Graphing the Hill Equation |
44:43 | |
| |
| The Slope and Degree of Cooperation |
46:25 | |
| |
| The Hill Coefficient |
49:48 | |
| |
| Hill Coefficient = 1 |
51:08 | |
| |
| Hill Coefficient < 1 |
55:55 | |
| |
| Where the Graph Hits the x-axis |
56:11 | |
| |
| Graph for Hemoglobin |
58:02 | |
|
Protein Function III: More on Hemoglobin |
1:07:16 |
| |
Intro |
0:00 | |
| |
Protein Function III: More on Hemoglobin |
0:11 | |
| |
| Two Models for Cooperative Binding: MWC & Sequential Model |
0:12 | |
| |
| MWC Model |
1:31 | |
| |
| Hemoglobin Subunits |
3:32 | |
| |
| Sequential Model |
8:00 | |
| |
| Hemoglobin Transports H⁺ & CO₂ |
17:23 | |
| |
| Binding Sites of H⁺ and CO₂ |
19:36 | |
| |
| CO₂ is Converted to Bicarbonate |
23:28 | |
| |
| Production of H⁺ & CO₂ in Tissues |
27:28 | |
| |
| H⁺ & CO₂ Binding are Inversely Related to O₂ Binding |
28:31 | |
| |
| The H⁺ Bohr Effect: His¹⁴⁶ Residue on the β Subunits |
33:31 | |
| |
| Heterotropic Allosteric Regulation of O₂ Binding by 2,3-Biphosphoglycerate (2,3 BPG) |
39:53 | |
| |
| Binding Curve for 2,3 BPG |
56:21 | |
Section 5: Enzymes |
|
Enzymes I |
41:38 |
| |
Intro |
0:00 | |
| |
Enzymes I |
0:38 | |
| |
| Enzymes Overview |
0:39 | |
| |
| Cofactor |
4:38 | |
| |
| Holoenzyme |
5:52 | |
| |
| Apoenzyme |
6:40 | |
| |
| Riboflavin, FAD, Pyridoxine, Pyridoxal Phosphate Structures |
7:28 | |
| |
| Carbonic Anhydrase |
8:45 | |
| |
| Classification of Enzymes |
9:55 | |
| |
| Example: EC 1.1.1.1 |
13:04 | |
| |
| Reaction of Oxidoreductases |
16:23 | |
| |
| Enzymes: Catalysts, Active Site, and Substrate |
18:28 | |
| |
| Illustration of Enzymes, Substrate, and Active Site |
27:22 | |
| |
| Catalysts & Activation Energies |
29:57 | |
| |
| Intermediates |
36:00 | |
|
Enzymes II |
44:02 |
| |
Intro |
0:00 | |
| |
Enzymes II: Transitions State, Binding Energy, & Induced Fit |
0:18 | |
| |
| Enzymes 'Fitting' Well With The Transition State |
0:20 | |
| |
| Example Reaction: Breaking of a Stick |
3:40 | |
| |
| Another Energy Diagram |
8:20 | |
| |
| Binding Energy |
9:48 | |
| |
| Enzymes Specificity |
11:03 | |
| |
| Key Point: Optimal Interactions Between Substrate & Enzymes |
15:15 | |
| |
| Induced Fit |
16:25 | |
| |
| Illustrations: Induced Fit |
20:58 | |
| |
Enzymes II: Catalytic Mechanisms |
22:17 | |
| |
| General Acid/Base Catalysis |
23:56 | |
| |
| Acid Form & Base Form of Amino Acid: Glu &Asp |
25:26 | |
| |
| Acid Form & Base Form of Amino Acid: Lys & Arg |
26:30 | |
| |
| Acid Form & Base Form of Amino Acid: Cys |
26:51 | |
| |
| Acid Form & Base Form of Amino Acid: His |
27:30 | |
| |
| Acid Form & Base Form of Amino Acid: Ser |
28:16 | |
| |
| Acid Form & Base Form of Amino Acid: Tyr |
28:30 | |
| |
| Example: Phosphohexose Isomerase |
29:20 | |
| |
| Covalent Catalysis |
34:19 | |
| |
| Example: Glyceraldehyde 3-Phosphate Dehydrogenase |
35:34 | |
| |
| Metal Ion Catalysis: Isocitrate Dehydrogenase |
38:45 | |
| |
| Function of Mn²⁺ |
42:15 | |
|
Enzymes III: Kinetics |
56:40 |
| |
Intro |
0:00 | |
| |
Enzymes III: Kinetics |
1:40 | |
| |
| Rate of an Enzyme-Catalyzed Reaction & Substrate Concentration |
1:41 | |
| |
| Graph: Substrate Concentration vs. Reaction Rate |
10:43 | |
| |
| Rate At Low and High Substrate Concentration |
14:26 | |
| |
| Michaelis & Menten Kinetics |
20:16 | |
| |
| More On Rate & Concentration of Substrate |
22:46 | |
| |
| Steady-State Assumption |
26:02 | |
| |
| Rate is Determined by How Fast ES Breaks Down to Product |
31:36 | |
| |
| Total Enzyme Concentration: [Et] = [E] + [ES] |
35:35 | |
| |
| Rate of ES Formation |
36:44 | |
| |
| Rate of ES Breakdown |
38:40 | |
| |
| Measuring Concentration of Enzyme-Substrate Complex |
41:19 | |
| |
| Measuring Initial & Maximum Velocity |
43:43 | |
| |
| Michaelis & Menten Equation |
46:44 | |
| |
| What Happens When V₀ = (1/2) Vmax? |
49:12 | |
| |
| When [S] << Km |
53:32 | |
| |
| When [S] >> Km |
54:44 | |
|
Enzymes IV: Lineweaver-Burk Plots |
20:37 |
| |
Intro |
0:00 | |
| |
Enzymes IV: Lineweaver-Burk Plots |
0:45 | |
| |
| Deriving The Lineweaver-Burk Equation |
0:46 | |
| |
| Lineweaver-Burk Plots |
3:55 | |
| |
| Example 1: Carboxypeptidase A |
8:00 | |
| |
| More on Km, Vmax, and Enzyme-catalyzed Reaction |
15:54 | |
|
Enzymes V: Enzyme Inhibition |
51:37 |
| |
Intro |
0:00 | |
| |
Enzymes V: Enzyme Inhibition Overview |
0:42 | |
| |
| Enzyme Inhibitors Overview |
0:43 | |
| |
| Classes of Inhibitors |
2:32 | |
| |
Competitive Inhibition |
3:08 | |
| |
| Competitive Inhibition |
3:09 | |
| |
| Michaelis & Menten Equation in the Presence of a Competitive Inhibitor |
7:40 | |
| |
| Double-Reciprocal Version of the Michaelis & Menten Equation |
14:48 | |
| |
| Competitive Inhibition Graph |
16:37 | |
| |
Uncompetitive Inhibition |
19:23 | |
| |
| Uncompetitive Inhibitor |
19:24 | |
| |
| Michaelis & Menten Equation for Uncompetitive Inhibition |
22:10 | |
| |
| The Lineweaver-Burk Equation for Uncompetitive Inhibition |
26:04 | |
| |
| Uncompetitive Inhibition Graph |
27:42 | |
| |
Mixed Inhibition |
30:30 | |
| |
| Mixed Inhibitor |
30:31 | |
| |
| Double-Reciprocal Version of the Equation |
33:34 | |
| |
| The Lineweaver-Burk Plots for Mixed Inhibition |
35:02 | |
| |
Summary of Reversible Inhibitor Behavior |
38:00 | |
| |
| Summary of Reversible Inhibitor Behavior |
38:01 | |
| |
| Note: Non-Competitive Inhibition |
42:22 | |
| |
Irreversible Inhibition |
45:15 | |
| |
| Irreversible Inhibition |
45:16 | |
| |
| Penicillin & Transpeptidase Enzyme |
46:50 | |
|
Enzymes VI: Regulatory Enzymes |
51:23 |
| |
Intro |
0:00 | |
| |
Enzymes VI: Regulatory Enzymes |
0:45 | |
| |
| Regulatory Enzymes Overview |
0:46 | |
| |
| Example: Glycolysis |
2:27 | |
| |
| Allosteric Regulatory Enzyme |
9:19 | |
| |
| Covalent Modification |
13:08 | |
| |
| Two Other Regulatory Processes |
16:28 | |
| |
| Allosteric Regulation |
20:58 | |
| |
| Feedback Inhibition |
25:12 | |
| |
| Feedback Inhibition Example: L-Threonine → L-Isoleucine |
26:03 | |
| |
| Covalent Modification |
27:26 | |
| |
| Covalent Modulators: -PO₃²⁻ |
29:30 | |
| |
| Protein Kinases |
31:59 | |
| |
| Protein Phosphatases |
32:47 | |
| |
| Addition/Removal of -PO₃²⁻ and the Effect on Regulatory Enzyme |
33:36 | |
| |
| Phosphorylation Sites of a Regulatory Enzyme |
38:38 | |
| |
| Proteolytic Cleavage |
41:48 | |
| |
| Zymogens: Chymotrypsin & Trypsin |
43:58 | |
| |
| Enzymes That Use More Than One Regulatory Process: Bacterial Glutamine Synthetase |
48:59 | |
| |
| Why The Complexity? |
50:27 | |
|
Enzymes VII: Km & Kcat |
54:49 |
| |
Intro |
0:00 | |
| |
Km |
1:48 | |
| |
| Recall the MichaelisMenten Equation |
1:49 | |
| |
| Km & Enzyme's Affinity |
6:18 | |
| |
| Rate Forward, Rate Backward, and Equilibrium Constant |
11:08 | |
| |
| When an Enzyme's Affinity for Its Substrate is High |
14:17 | |
| |
| More on Km & Enzyme Affinity |
17:29 | |
| |
| The Measure of Km Under MichaelisMenten kinetic |
23:19 | |
| |
Kcat (First-order Rate Constant or Catalytic Rate Constant) |
24:10 | |
| |
| Kcat: Definition |
24:11 | |
| |
| Kcat & The MichaelisMenten Postulate |
25:18 | |
| |
| Finding Vmax and [Et} |
27:27 | |
| |
| Units for Vmax and Kcat |
28:26 | |
| |
| Kcat: Turnover Number |
28:55 | |
| |
| MichaelisMenten Equation |
32:12 | |
| |
Km & Kcat |
36:37 | |
| |
| Second Order Rate Equation |
36:38 | |
| |
| (Kcat)/(Km): Overview |
39:22 | |
| |
| High (Kcat)/(Km) |
40:20 | |
| |
| Low (Kcat)/(Km) |
43:16 | |
| |
| Practical Big Picture |
46:28 | |
| |
| Upper Limit to (Kcat)/(Km) |
48:56 | |
| |
| More On Kcat and Km |
49:26 | |
Section 6: Carbohydrates |
|
Monosaccharides |
1:17:46 |
| |
Intro |
0:00 | |
| |
Monosaccharides |
1:49 | |
| |
| Carbohydrates Overview |
1:50 | |
| |
| Three Major Classes of Carbohydrates |
4:48 | |
| |
| Definition of Monosaccharides |
5:46 | |
| |
Examples of Monosaccharides: Aldoses |
7:06 | |
| |
| D-Glyceraldehyde |
7:39 | |
| |
| D-Erythrose |
9:00 | |
| |
| D-Ribose |
10:10 | |
| |
| D-Glucose |
11:20 | |
| |
| Observation: Aldehyde Group |
11:54 | |
| |
| Observation: Carbonyl 'C' |
12:30 | |
| |
| Observation: D & L Naming System |
12:54 | |
| |
Examples of Monosaccharides: Ketose |
16:54 | |
| |
| Dihydroxy Acetone |
17:28 | |
| |
| D-Erythrulose |
18:30 | |
| |
| D-Ribulose |
19:49 | |
| |
| D-Fructose |
21:10 | |
| |
| D-Glucose Comparison |
23:18 | |
| |
| More information of Ketoses |
24:50 | |
| |
| Let's Look Closer at D-Glucoses |
25:50 | |
| |
Let's Look At All the D-Hexose Stereoisomers |
31:22 | |
| |
| D-Allose |
32:20 | |
| |
| D-Altrose |
33:01 | |
| |
| D-Glucose |
33:39 | |
| |
| D-Gulose |
35:00 | |
| |
| D-Mannose |
35:40 | |
| |
| D-Idose |
36:42 | |
| |
| D-Galactose |
37:14 | |
| |
| D-Talose |
37:42 | |
| |
Epimer |
40:05 | |
| |
| Definition of Epimer |
40:06 | |
| |
| Example of Epimer: D-Glucose, D-Mannose, and D-Galactose |
40:57 | |
| |
Hemiacetal or Hemiketal |
44:36 | |
| |
| Hemiacetal/Hemiketal Overview |
45:00 | |
| |
| Ring Formation of the α and β Configurations of D-Glucose |
50:52 | |
| |
| Ring Formation of the α and β Configurations of Fructose |
61:39 | |
| |
Haworth Projection |
67:34 | |
| |
| Pyranose & Furanose Overview |
67:38 | |
| |
| Haworth Projection: Pyranoses |
69:30 | |
| |
| Haworth Projection: Furanose |
74:56 | |
|
Hexose Derivatives & Reducing Sugars |
37:06 |
| |
Intro |
0:00 | |
| |
Hexose Derivatives |
0:15 | |
| |
| Point of Clarification: Forming a Cyclic Sugar From a Linear Sugar |
0:16 | |
| |
| Let's Recall the α and β Anomers of Glucose |
8:42 | |
| |
| α-Glucose |
10:54 | |
| |
Hexose Derivatives that Play Key Roles in Physiology Progression |
17:38 | |
| |
| β-Glucose |
18:24 | |
| |
| β-Glucosamine |
18:48 | |
| |
| N-Acetyl-β-Glucosamine |
20:14 | |
| |
| β-Glucose-6-Phosphate |
22:22 | |
| |
| D-Gluconate |
24:10 | |
| |
| Glucono-δ-Lactone |
26:33 | |
| |
Reducing Sugars |
29:50 | |
| |
| Reducing Sugars Overview |
29:51 | |
| |
| Reducing Sugars Example: β-Galactose |
32:36 | |
|
Disaccharides |
43:32 |
| |
Intro |
0:00 | |
| |
Disaccharides |
0:15 | |
| |
| Disaccharides Overview |
0:19 | |
| |
| Examples of Disaccharides & How to Name Them |
2:49 | |
| |
| Disaccharides Trehalose Overview |
15:46 | |
| |
| Disaccharides Trehalose: Flip |
20:52 | |
| |
| Disaccharides Trehalose: Spin |
28:36 | |
| |
| Example: Draw the Structure |
33:12 | |
|
Polysaccharides |
39:25 |
| |
Intro |
0:00 | |
| |
Recap Example: Draw the Structure of Gal(α1↔β1)Man |
0:38 | |
| |
Polysaccharides |
9:46 | |
| |
| Polysaccharides Overview |
9:50 | |
| |
| Homopolysaccharide |
13:12 | |
| |
| Heteropolysaccharide |
13:47 | |
| |
| Homopolysaccharide as Fuel Storage |
16:23 | |
| |
| Starch Has Two Types of Glucose Polymer: Amylose |
17:10 | |
| |
| Starch Has Two Types of Glucose Polymer: Amylopectin |
18:04 | |
| |
| Polysaccharides: Reducing End & Non-Reducing End |
19:30 | |
| |
| Glycogen |
20:06 | |
| |
| Examples: Structures of Polysaccharides |
21:42 | |
| |
| Let's Draw an (α1→4) & (α1→6) of Amylopectin by Hand. |
28:14 | |
| |
| More on Glycogen |
31:17 | |
| |
| Glycogen, Concentration, & The Concept of Osmolarity |
35:16 | |
|
Polysaccharides, Part 2 |
44:15 |
| |
Intro |
0:00 | |
| |
Polysaccharides |
0:17 | |
| |
| Example: Cellulose |
0:34 | |
| |
| Glycoside Bond |
7:25 | |
| |
| Example Illustrations |
12:30 | |
| |
| Glycosaminoglycans Part 1 |
15:55 | |
| |
| Glycosaminoglycans Part 2 |
18:34 | |
| |
| Glycosaminoglycans & Sulfate Attachments |
22:42 | |
| |
| β-D-N-Acetylglucosamine |
24:49 | |
| |
| β-D-N-AcetylGalactosamine |
25:42 | |
| |
| β-D-Glucuronate |
26:44 | |
| |
| β-L-Iduronate |
27:54 | |
| |
| More on Sulfate Attachments |
29:49 | |
| |
| Hylarunic Acid |
32:00 | |
| |
| Hyaluronates |
39:32 | |
| |
| Other Glycosaminoglycans |
40:46 | |
|
Glycoconjugates |
44:23 |
| |
Intro |
0:00 | |
| |
Glycoconjugates |
0:24 | |
| |
| Overview |
0:25 | |
| |
| Proteoglycan |
2:53 | |
| |
| Glycoprotein |
5:20 | |
| |
| Glycolipid |
7:25 | |
| |
| Proteoglycan vs. Glycoprotein |
8:15 | |
| |
| Cell Surface Diagram |
11:17 | |
| |
| Proteoglycan Common Structure |
14:24 | |
| |
| Example: Chondroitin-4-Sulfate |
15:06 | |
| |
| Glycoproteins |
19:50 | |
| |
| The Monomers that Commonly Show Up in The Oligo Portions of Glycoproteins |
28:02 | |
| |
| N-Acetylneuraminic Acid |
31:17 | |
| |
| L-Furose |
32:37 | |
| |
| Example of an N-Linked Oligosaccharide |
33:21 | |
| |
| Cell Membrane Structure |
36:35 | |
| |
| Glycolipids & Lipopolysaccharide |
37:22 | |
| |
| Structure Example |
41:28 | |
|
More Example Problems with Carbohydrates |
40:22 |
| |
Intro |
0:00 | |
| |
Example 1 |
1:09 | |
| |
Example 2 |
2:34 | |
| |
Example 3 |
5:12 | |
| |
Example 4 |
16:19 | |
| |
| Question |
16:20 | |
| |
| Solution |
17:25 | |
| |
Example 5 |
24:18 | |
| |
| Question |
24:19 | |
| |
| Structure of 2,3-Di-O-Methylglucose |
26:47 | |
| |
| Part A |
28:11 | |
| |
| Part B |
33:46 | |
Section 7: Lipids |
|
Fatty Acids & Triacylglycerols |
54:55 |
| |
Intro |
0:00 | |
| |
Fatty Acids |
0:32 | |
| |
| Lipids Overview |
0:34 | |
| |
| Introduction to Fatty Acid |
3:18 | |
| |
| Saturated Fatty Acid |
6:13 | |
| |
| Unsaturated or Polyunsaturated Fatty Acid |
7:07 | |
| |
| Saturated Fatty Acid Example |
7:46 | |
| |
| Unsaturated Fatty Acid Example |
9:06 | |
| |
| Notation Example: Chain Length, Degree of Unsaturation, & Double Bonds Location of Fatty Acid |
11:56 | |
| |
| Example 1: Draw the Structure |
16:18 | |
| |
| Example 2: Give the Shorthand for cis,cis-5,8-Hexadecadienoic Acid |
20:12 | |
| |
| Example 3 |
23:12 | |
| |
| Solubility of Fatty Acids |
25:45 | |
| |
| Melting Points of Fatty Acids |
29:40 | |
| |
Triacylglycerols |
34:13 | |
| |
| Definition of Triacylglycerols |
34:14 | |
| |
| Structure of Triacylglycerols |
35:08 | |
| |
| Example: Triacylglycerols |
40:23 | |
| |
| Recall Ester Formation |
43:57 | |
| |
| The Body's Primary Fuel-Reserves |
47:22 | |
| |
| Two Primary Advantages to Storing Energy as Triacylglycerols Instead of Glycogen: Number 1 |
49:24 | |
| |
| Two Primary Advantages to Storing Energy as Triacylglycerols Instead of Glycogen: Number 2 |
51:54 | |
|
Membrane Lipids |
38:51 |
| |
Intro |
0:00 | |
| |
Membrane Lipids |
0:26 | |
| |
| Definition of Membrane Lipids |
0:27 | |
| |
| Five Major Classes of Membrane Lipids |
2:38 | |
| |
Glycerophospholipids |
5:04 | |
| |
| Glycerophospholipids Overview |
5:05 | |
| |
| The X Group |
8:05 | |
| |
| Example: Phosphatidyl Ethanolamine |
10:51 | |
| |
| Example: Phosphatidyl Choline |
13:34 | |
| |
| Phosphatidyl Serine |
15:16 | |
| |
| Head Groups |
16:50 | |
| |
| Ether Linkages Instead of Ester Linkages |
20:05 | |
| |
Galactolipids |
23:39 | |
| |
| Galactolipids Overview |
23:40 | |
| |
| Monogalactosyldiacylglycerol: MGDG |
25:17 | |
| |
| Digalactosyldiacylglycerol: DGDG |
28:13 | |
| |
| Structure Examples 1: Lipid Bilayer |
31:35 | |
| |
| Structure Examples 2: Cross Section of a Cell |
34:56 | |
| |
| Structure Examples 3: MGDG & DGDG |
36:28 | |
|
Membrane Lipids, Part 2 |
38:20 |
| |
Intro |
0:00 | |
| |
Sphingolipids |
0:11 | |
| |
| Sphingolipid Overview |
0:12 | |
| |
| Sphingosine Structure |
1:42 | |
| |
| Ceramide |
3:56 | |
| |
| Subclasses of Sphingolipids Overview |
6:00 | |
| |
Subclasses of Sphingolipids: Sphingomyelins |
7:53 | |
| |
| Sphingomyelins |
7:54 | |
| |
Subclasses of Sphingolipids: Glycosphingolipid |
12:47 | |
| |
| Glycosphingolipid Overview |
12:48 | |
| |
| Cerebrosides & Globosides Overview |
14:33 | |
| |
| Example: Cerebrosides |
15:43 | |
| |
| Example: Globosides |
17:14 | |
| |
Subclasses of Sphingolipids: Gangliosides |
19:07 | |
| |
| Gangliosides |
19:08 | |
| |
| Medical Application: Tay-Sachs Disease |
23:34 | |
| |
Sterols |
30:45 | |
| |
| Sterols: Basic Structure |
30:46 | |
| |
| Important Example: Cholesterol |
32:01 | |
| |
| Structures Example |
34:13 | |
|
The Biologically Active Lipids |
48:36 |
| |
Intro |
0:00 | |
| |
The Biologically Active Lipids |
0:44 | |
| |
| Phosphatidyl Inositol Structure |
0:45 | |
| |
| Phosphatidyl Inositol Reaction |
3:24 | |
| |
| Image Example |
12:49 | |
| |
| Eicosanoids |
14:12 | |
| |
| Arachidonic Acid & Membrane Lipid Containing Arachidonic Acid |
18:41 | |
| |
Three Classes of Eicosanoids |
20:42 | |
| |
| Overall Structures |
21:38 | |
| |
| Prostagladins |
22:56 | |
| |
| Thromboxane |
27:19 | |
| |
| Leukotrienes |
30:19 | |
| |
More On The Biologically Active Lipids |
33:34 | |
| |
| Steroid Hormones |
33:35 | |
| |
| Fat Soluble Vitamins |
38:25 | |
| |
| Vitamin D₃ |
40:40 | |
| |
| Vitamin A |
43:17 | |
| |
| Vitamin E |
45:12 | |
| |
| Vitamin K |
47:17 | |
Section 8: Energy & Biological Systems (Bioenergetics) |
|
Thermodynamics, Free Energy & Equilibrium |
45:51 |
| |
Intro |
0:00 | |
| |
Thermodynamics, Free Energy and Equilibrium |
1:03 | |
| |
| Reaction: Glucose + Pi → Glucose 6-Phosphate |
1:50 | |
| |
| Thermodynamics & Spontaneous Processes |
3:31 | |
| |
| In Going From Reactants → Product, a Reaction Wants to Release Heat |
6:30 | |
| |
| A Reaction Wants to Become More Disordered |
9:10 | |
| |
| ∆H < 0 |
10:30 | |
| |
| ∆H > 0 |
10:57 | |
| |
| ∆S > 0 |
11:23 | |
| |
| ∆S <0 |
11:56 | |
| |
| ∆G = ∆H - T∆S at Constant Pressure |
12:15 | |
| |
| Gibbs Free Energy |
15:00 | |
| |
| ∆G < 0 |
16:49 | |
| |
| ∆G > 0 |
17:07 | |
| |
| Reference Frame For Thermodynamics Measurements |
17:57 | |
| |
| More On BioChemistry Standard |
22:36 | |
| |
| Spontaneity |
25:36 | |
| |
| Keq |
31:45 | |
| |
| Example: Glucose + Pi → Glucose 6-Phosphate |
34:14 | |
| |
Example Problem 1 |
40:25 | |
| |
| Question |
40:26 | |
| |
| Solution |
41:12 | |
|
More on Thermodynamics & Free Energy |
37:06 |
| |
Intro |
0:00 | |
| |
More on Thermodynamics & Free Energy |
0:16 | |
| |
| Calculating ∆G Under Standard Conditions |
0:17 | |
| |
| Calculating ∆G Under Physiological Conditions |
2:05 | |
| |
| ∆G < 0 |
5:39 | |
| |
| ∆G = 0 |
7:03 | |
| |
| Reaction Moving Forward Spontaneously |
8:00 | |
| |
| ∆G & The Maximum Theoretical Amount of Free Energy Available |
10:36 | |
| |
| Example Problem 1 |
13:11 | |
| |
| Reactions That Have Species in Common |
17:48 | |
| |
| Example Problem 2: Part 1 |
20:10 | |
| |
| Example Problem 2: Part 2- Enzyme Hexokinase & Coupling |
25:08 | |
| |
| Example Problem 2: Part 3 |
30:34 | |
| |
| Recap |
34:45 | |
|
ATP & Other High-Energy Compounds |
44:32 |
| |
Intro |
0:00 | |
| |
ATP & Other High-Energy Compounds |
0:10 | |
| |
| Endergonic Reaction Coupled With Exergonic Reaction |
0:11 | |
| |
| Major Theme In Metabolism |
6:56 | |
| |
Why the ∆G°' for ATP Hydrolysis is Large & Negative |
12:24 | |
| |
| ∆G°' for ATP Hydrolysis |
12:25 | |
| |
| Reason 1: Electrostatic Repulsion |
14:24 | |
| |
| Reason 2: Pi & Resonance Forms |
15:33 | |
| |
| Reason 3: Concentrations of ADP & Pi |
17:32 | |
| |
ATP & Other High-Energy Compounds Cont'd |
18:48 | |
| |
| More On ∆G°' & Hydrolysis |
18:49 | |
| |
| Other Compounds That Have Large Negative ∆G°' of Hydrolysis: Phosphoenol Pyruvate (PEP) |
25:14 | |
| |
| Enzyme Pyruvate Kinase |
30:36 | |
| |
| Another High Energy Molecule: 1,3 Biphosphoglycerate |
36:17 | |
| |
| Another High Energy Molecule: Phophocreatine |
39:41 | |
|
Phosphoryl Group Transfers |
30:08 |
| |
Intro |
0:00 | |
| |
Phosphoryl Group Transfer |
0:27 | |
| |
| Phosphoryl Group Transfer Overview |
0:28 | |
| |
| Example: Glutamate → Glutamine Part 1 |
7:11 | |
| |
| Example: Glutamate → Glutamine Part 2 |
13:29 | |
| |
| ATP Not Only Transfers Phosphoryl, But Also Pyrophosphoryl & Adenylyl Groups |
17:03 | |
| |
| Attack At The γ Phosphorous Transfers a Phosphoryl |
19:02 | |
| |
| Attack At The β Phosphorous Gives Pyrophosphoryl |
22:44 | |
|
Oxidation-Reduction Reactions |
49:46 |
| |
Intro |
0:00 | |
| |
Oxidation-Reduction Reactions |
1:32 | |
| |
| Redox Reactions |
1:33 | |
| |
| Example 1: Mg + Al³⁺ → Mg²⁺ + Al |
3:49 | |
| |
| Reduction Potential Definition |
10:47 | |
| |
| Reduction Potential Example |
13:38 | |
| |
| Organic Example |
22:23 | |
| |
| Review: How To Find The Oxidation States For Carbon |
24:15 | |
| |
Examples: Oxidation States For Carbon |
27:45 | |
| |
| Example 1: Oxidation States For Carbon |
27:46 | |
| |
| Example 2: Oxidation States For Carbon |
28:36 | |
| |
| Example 3: Oxidation States For Carbon |
29:18 | |
| |
| Example 4: Oxidation States For Carbon |
29:44 | |
| |
| Example 5: Oxidation States For Carbon |
30:10 | |
| |
| Example 6: Oxidation States For Carbon |
30:40 | |
| |
| Example 7: Oxidation States For Carbon |
31:20 | |
| |
| Example 8: Oxidation States For Carbon |
32:10 | |
| |
| Example 9: Oxidation States For Carbon |
32:52 | |
| |
Oxidation-Reduction Reactions, cont'd |
35:22 | |
| |
| More On Reduction Potential |
35:28 | |
| |
| Lets' Start With ∆G = ∆G°' + RTlnQ |
38:29 | |
| |
| Example: Oxidation Reduction Reactions |
41:42 | |
|
More On Oxidation-Reduction Reactions |
56:34 |
| |
Intro |
0:00 | |
| |
More On Oxidation-Reduction Reactions |
0:10 | |
| |
| Example 1: What If the Concentrations Are Not Standard? |
0:11 | |
| |
| Alternate Procedure That Uses The 1/2 Reactions Individually |
8:57 | |
| |
| Universal Electron Carriers in Aqueous Medium: NAD+ & NADH |
15:12 | |
| |
| The Others Are
|
19:22 | |
| |
| NAD+ & NADP Coenzymes |
20:56 | |
| |
| FMN & FAD |
22:03 | |
| |
| Nicotinamide Adenine Dinucleotide (Phosphate) |
23:03 | |
| |
| Reduction 1/2 Reactions |
36:10 | |
| |
| Ratio of NAD+ : NADH |
36:52 | |
| |
| Ratio of NADPH : NADP+ |
38:02 | |
| |
| Specialized Roles of NAD+ & NADPH |
38:48 | |
| |
| Oxidoreductase Enzyme Overview |
40:26 | |
| |
| Examples of Oxidoreductase |
43:32 | |
| |
| The Flavin Nucleotides |
46:46 | |
|
Example Problems For Bioenergetics |
42:12 |
| |
Intro |
0:00 | |
| |
Example 1: Calculate the ∆G°' For The Following Reaction |
1:04 | |
| |
| Example 1: Question |
1:05 | |
| |
| Example 1: Solution |
2:20 | |
| |
Example 2: Calculate the Keq For the Following |
4:20 | |
| |
| Example 2: Question |
4:21 | |
| |
| Example 2: Solution |
5:54 | |
| |
Example 3: Calculate the ∆G°' For The Hydrolysis of ATP At 25°C |
8:52 | |
| |
| Example 3: Question |
8:53 | |
| |
| Example 3: Solution |
10:30 | |
| |
| Example 3: Alternate Procedure |
13:48 | |
| |
Example 4: Problems For Bioenergetics |
16:46 | |
| |
| Example 4: Questions |
16:47 | |
| |
| Example 4: Part A Solution |
21:19 | |
| |
| Example 4: Part B Solution |
23:26 | |
| |
| Example 4: Part C Solution |
26:12 | |
| |
Example 5: Problems For Bioenergetics |
29:27 | |
| |
| Example 5: Questions |
29:35 | |
| |
| Example 5: Solution - Part 1 |
32:16 | |
| |
| Example 5: Solution - Part 2 |
34:39 | |
Section 9: Glycolysis and Gluconeogenesis |
|
Overview of Glycolysis I |
43:32 |
| |
Intro |
0:00 | |
| |
Overview of Glycolysis |
0:48 | |
| |
| Three Primary Paths For Glucose |
1:04 | |
| |
| Preparatory Phase of Glycolysis |
4:40 | |
| |
| Payoff Phase of Glycolysis |
6:40 | |
| |
| Glycolysis Reactions Diagram |
7:58 | |
| |
| Enzymes of Glycolysis |
12:41 | |
| |
Glycolysis Reactions |
16:02 | |
| |
| Step 1 |
16:03 | |
| |
| Step 2 |
18:03 | |
| |
| Step 3 |
18:52 | |
| |
| Step 4 |
20:08 | |
| |
| Step 5 |
21:42 | |
| |
| Step 6 |
22:44 | |
| |
| Step 7 |
24:22 | |
| |
| Step 8 |
25:11 | |
| |
| Step 9 |
26:00 | |
| |
| Step 10 |
26:51 | |
| |
Overview of Glycolysis Cont. |
27:28 | |
| |
| The Overall Reaction for Glycolysis |
27:29 | |
| |
| Recall The High-Energy Phosphorylated Compounds Discusses In The Bioenergetics Unit |
33:10 | |
| |
| What Happens To The Pyruvate That Is Formed? |
37:58 | |
|
Glycolysis II |
1:01:47 |
| |
Intro |
0:00 | |
| |
Glycolysis Step 1: The Phosphorylation of Glucose |
0:27 | |
| |
| Glycolysis Step 1: Reaction |
0:28 | |
| |
| Hexokinase |
2:28 | |
| |
| Glycolysis Step 1: Mechanism-Simple Nucleophilic Substitution |
6:34 | |
| |
Glycolysis Step 2: Conversion of Glucose 6-Phosphate → Fructose 6-Phosphate |
11:33 | |
| |
| Glycolysis Step 2: Reaction |
11:34 | |
| |
| Glycolysis Step 2: Mechanism, Part 1 |
14:40 | |
| |
| Glycolysis Step 2: Mechanism, Part 2 |
18:16 | |
| |
| Glycolysis Step 2: Mechanism, Part 3 |
19:56 | |
| |
| Glycolysis Step 2: Mechanism, Part 4 (Ring Closing & Dissociation) |
21:54 | |
| |
Glycolysis Step 3: Conversion of Fructose 6-Phosphate to Fructose 1,6-Biphosphate |
24:16 | |
| |
| Glycolysis Step 3: Reaction |
24:17 | |
| |
| Glycolysis Step 3: Mechanism |
26:40 | |
| |
Glycolysis Step 4: Cleavage of Fructose 1,6-Biphosphate |
31:10 | |
| |
| Glycolysis Step 4: Reaction |
31:11 | |
| |
| Glycolysis Step 4: Mechanism, Part 1 (Binding & Ring Opening) |
35:26 | |
| |
| Glycolysis Step 4: Mechanism, Part 2 |
37:40 | |
| |
| Glycolysis Step 4: Mechanism, Part 3 |
39:30 | |
| |
| Glycolysis Step 4: Mechanism, Part 4 |
44:00 | |
| |
| Glycolysis Step 4: Mechanism, Part 5 |
46:34 | |
| |
| Glycolysis Step 4: Mechanism, Part 6 |
49:00 | |
| |
| Glycolysis Step 4: Mechanism, Part 7 |
50:12 | |
| |
| Hydrolysis of The Imine |
52:33 | |
| |
Glycolysis Step 5: Conversion of Dihydroxyaceton Phosphate to Glyceraldehyde 3-Phosphate |
55:38 | |
| |
| Glycolysis Step 5: Reaction |
55:39 | |
| |
Breakdown and Numbering of Sugar |
57:40 | |
|
Glycolysis III |
59:17 |
| |
Intro |
0:00 | |
| |
Glycolysis Step 5: Conversion of Dihydroxyaceton Phosphate to Glyceraldehyde 3-Phosphate |
0:44 | |
| |
| Glycolysis Step 5: Mechanism, Part 1 |
0:45 | |
| |
| Glycolysis Step 5: Mechanism, Part 2 |
3:53 | |
| |
Glycolysis Step 6: Oxidation of Glyceraldehyde 3-Phosphate to 1,3-Biphosphoglycerate |
5:14 | |
| |
| Glycolysis Step 6: Reaction |
5:15 | |
| |
| Glycolysis Step 6: Mechanism, Part 1 |
8:52 | |
| |
| Glycolysis Step 6: Mechanism, Part 2 |
12:58 | |
| |
| Glycolysis Step 6: Mechanism, Part 3 |
14:26 | |
| |
| Glycolysis Step 6: Mechanism, Part 4 |
16:23 | |
| |
Glycolysis Step 7: Phosphoryl Transfer From 1,3-Biphosphoglycerate to ADP to Form ATP |
19:08 | |
| |
| Glycolysis Step 7: Reaction |
19:09 | |
| |
| Substrate-Level Phosphorylation |
23:18 | |
| |
| Glycolysis Step 7: Mechanism (Nucleophilic Substitution) |
26:57 | |
| |
Glycolysis Step 8: Conversion of 3-Phosphoglycerate to 2-Phosphoglycerate |
28:44 | |
| |
| Glycolysis Step 8: Reaction |
28:45 | |
| |
| Glycolysis Step 8: Mechanism, Part 1 |
30:08 | |
| |
| Glycolysis Step 8: Mechanism, Part 2 |
32:24 | |
| |
| Glycolysis Step 8: Mechanism, Part 3 |
34:02 | |
| |
| Catalytic Cycle |
35:42 | |
| |
Glycolysis Step 9: Dehydration of 2-Phosphoglycerate to Phosphoenol Pyruvate |
37:20 | |
| |
| Glycolysis Step 9: Reaction |
37:21 | |
| |
| Glycolysis Step 9: Mechanism, Part 1 |
40:12 | |
| |
| Glycolysis Step 9: Mechanism, Part 2 |
42:01 | |
| |
| Glycolysis Step 9: Mechanism, Part 3 |
43:58 | |
| |
Glycolysis Step 10: Transfer of a Phosphoryl Group From Phosphoenol Pyruvate To ADP To Form ATP |
45:16 | |
| |
| Glycolysis Step 10: Reaction |
45:17 | |
| |
| Substrate-Level Phosphorylation |
48:32 | |
| |
| Energy Coupling Reaction |
51:24 | |
| |
Glycolysis Balance Sheet |
54:15 | |
| |
| Glycolysis Balance Sheet |
54:16 | |
| |
| 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 |
39:47 |
| |
Intro |
0:00 | |
| |
Feeder Pathways |
0:42 | |
| |
| Feeder Pathways Overview |
0:43 | |
| |
| Starch, Glycogen |
2:25 | |
| |
| Lactose |
4:38 | |
| |
| Galactose |
4:58 | |
| |
| Manose |
5:22 | |
| |
| Trehalose |
5:45 | |
| |
| Sucrose |
5:56 | |
| |
| Fructose |
6:07 | |
| |
Fates of Pyruvate: Aerobic & Anaerobic Conditions |
7:39 | |
| |
| Aerobic Conditions & Pyruvate |
7:40 | |
| |
| Anaerobic Fates of Pyruvate |
11:18 | |
| |
Fates of Pyruvate: Lactate Acid Fermentation |
14:10 | |
| |
| Lactate Acid Fermentation |
14:11 | |
| |
Fates of Pyruvate: Ethanol Fermentation |
19:01 | |
| |
| Ethanol Fermentation Reaction |
19:02 | |
| |
| TPP: Thiamine Pyrophosphate (Functions and Structure) |
23:10 | |
| |
| Ethanol Fermentation Mechanism, Part 1 |
27:53 | |
| |
| Ethanol Fermentation Mechanism, Part 2 |
29:06 | |
| |
| Ethanol Fermentation Mechanism, Part 3 |
31:15 | |
| |
| Ethanol Fermentation Mechanism, Part 4 |
32:44 | |
| |
| Ethanol Fermentation Mechanism, Part 5 |
34:33 | |
| |
| Ethanol Fermentation Mechanism, Part 6 |
35:48 | |
|
Gluconeogenesis I |
41:34 |
| |
Intro |
0:00 | |
| |
Gluconeogenesis, Part 1 |
1:02 | |
| |
| Gluconeogenesis Overview |
1:03 | |
| |
| 3 Glycolytic Reactions That Are Irreversible Under Physiological Conditions |
2:29 | |
| |
| Gluconeogenesis Reactions Overview |
6:17 | |
| |
| Reaction: Pyruvate to Oxaloacetate |
11:07 | |
| |
| Reaction: Oxaloacetate to Phosphoenolpyruvate (PEP) |
13:29 | |
| |
| First Pathway That Pyruvate Can Take to Become Phosphoenolpyruvate |
15:24 | |
| |
| Second Pathway That Pyruvate Can Take to Become Phosphoenolpyruvate |
21:00 | |
| |
| Transportation of Pyruvate From The Cytosol to The Mitochondria |
24:15 | |
| |
| Transportation Mechanism, Part 1 |
26:41 | |
| |
| Transportation Mechanism, Part 2 |
30:43 | |
| |
| Transportation Mechanism, Part 3 |
34:04 | |
| |
| Transportation Mechanism, Part 4 |
38:14 | |
|
Gluconeogenesis II |
34:18 |
| |
Intro |
0:00 | |
| |
Oxaloacetate → Phosphoenolpyruvate (PEP) |
0:35 | |
| |
| Mitochondrial Membrane Does Not Have a Transporter for Oxaloactate |
0:36 | |
| |
| Reaction: Oxaloacetate to Phosphoenolpyruvate (PEP) |
3:36 | |
| |
| Mechanism: Oxaloacetate to Phosphoenolpyruvate (PEP) |
4:48 | |
| |
| Overall Reaction: Pyruvate to Phosphoenolpyruvate |
7:01 | |
| |
| Recall The Two Pathways That Pyruvate Can Take to Become Phosphoenolpyruvate |
10:16 | |
| |
| NADH in Gluconeogenesis |
12:29 | |
| |
Second Pathway: Lactate → Pyruvate |
18:22 | |
| |
| Cytosolic PEP Carboxykinase, Mitochondrial PEP Carboxykinase, & Isozymes |
18:23 | |
| |
| 2nd Bypass Reaction |
23:04 | |
| |
| 3rd Bypass Reaction |
24:01 | |
| |
| Overall Process |
25:17 | |
| |
Other Feeder Pathways For Gluconeogenesis |
26:35 | |
| |
| Carbon Intermediates of The Citric Acid Cycle |
26:36 | |
| |
| Amino Acids & The Gluconeogenic Pathway |
29:45 | |
| |
| Glycolysis & Gluconeogenesis Are Reciprocally Regulated |
32:00 | |
|
The Pentose Phosphate Pathway |
42:52 |
| |
Intro |
0:00 | |
| |
The Pentose Phosphate Pathway Overview |
0:17 | |
| |
| The Major Fate of Glucose-6-Phosphate |
0:18 | |
| |
| The Pentose Phosphate Pathway (PPP) Overview |
1:00 | |
| |
Oxidative Phase of The Pentose Phosphate Pathway |
4:33 | |
| |
| Oxidative Phase of The Pentose Phosphate Pathway: Reaction Overview |
4:34 | |
| |
| Ribose-5-Phosphate: Glutathione & Reductive Biosynthesis |
9:02 | |
| |
| Glucose-6-Phosphate to 6-Phosphogluconate |
12:48 | |
| |
| 6-Phosphogluconate to Ribulose-5-Phosphate |
15:39 | |
| |
| Ribulose-5-Phosphate to Ribose-5-Phosphate |
17:05 | |
| |
Non-Oxidative Phase of The Pentose Phosphate Pathway |
19:55 | |
| |
| Non-Oxidative Phase of The Pentose Phosphate Pathway: Overview |
19:56 | |
| |
| General Transketolase Reaction |
29:03 | |
| |
| Transaldolase Reaction |
35:10 | |
| |
| Final Transketolase Reaction |
39:10 | |
Section 10: The Citric Acid Cycle (Krebs Cycle) |
|
Citric Acid Cycle I |
36:10 |
| |
Intro |
0:00 | |
| |
Stages of Cellular Respiration |
0:23 | |
| |
| Stages of Cellular Respiration |
0:24 | |
| |
From Pyruvate to Acetyl-CoA |
6:56 | |
| |
| From Pyruvate to Acetyl-CoA: Pyruvate Dehydrogenase Complex |
6:57 | |
| |
| Overall Reaction |
8:42 | |
| |
| Oxidative Decarboxylation |
11:54 | |
| |
| Pyruvate Dehydrogenase (PDH) & Enzymes |
15:30 | |
| |
| Pyruvate Dehydrogenase (PDH) Requires 5 Coenzymes |
17:15 | |
| |
| Molecule of CoEnzyme A |
18:52 | |
| |
| Thioesters |
20:56 | |
| |
| Lipoic Acid |
22:31 | |
| |
| Lipoate Is Attached To a Lysine Residue On E₂ |
24:42 | |
| |
| Pyruvate Dehydrogenase Complex: Reactions |
26:36 | |
| |
| E1: Reaction 1 & 2 |
30:38 | |
| |
| E2: Reaction 3 |
31:58 | |
| |
| E3: Reaction 4 & 5 |
32:44 | |
| |
| Substrate Channeling |
34:17 | |
|
Citric Acid Cycle II |
49:20 |
| |
Intro |
0:00 | |
| |
Citric Acid Cycle Reactions Overview |
0:26 | |
| |
| Citric Acid Cycle Reactions Overview: Part 1 |
0:27 | |
| |
| Citric Acid Cycle Reactions Overview: Part 2 |
7:03 | |
| |
| Things to Note |
10:58 | |
| |
Citric Acid Cycle Reactions & Mechanism |
13:57 | |
| |
| Reaction 1: Formation of Citrate |
13:58 | |
| |
| Reaction 1: Mechanism |
19:01 | |
| |
| Reaction 2: Citrate to Cis Aconistate to Isocitrate |
28:50 | |
| |
| Reaction 3: Isocitrate to α-Ketoglutarate |
32:35 | |
| |
| Reaction 3: Two Isocitrate Dehydrogenase Enzymes |
36:24 | |
| |
| Reaction 3: Mechanism |
37:33 | |
| |
| Reaction 4: Oxidation of α-Ketoglutarate to Succinyl-CoA |
41:38 | |
| |
| Reaction 4: Notes |
46:34 | |
|
Citric Acid Cycle III |
44:11 |
| |
Intro |
0:00 | |
| |
Citric Acid Cycle Reactions & Mechanism |
0:21 | |
| |
| Reaction 5: Succinyl-CoA to Succinate |
0:24 | |
| |
| Reaction 5: Reaction Sequence |
2:35 | |
| |
| Reaction 6: Oxidation of Succinate to Fumarate |
8:28 | |
| |
| Reaction 7: Fumarate to Malate |
10:17 | |
| |
| Reaction 8: Oxidation of L-Malate to Oxaloacetate |
14:15 | |
| |
More On The Citric Acid Cycle |
17:17 | |
| |
| Energy from Oxidation |
17:18 | |
| |
| How Can We Transfer This NADH Into the Mitochondria |
27:10 | |
| |
| Citric Cycle is Amphibolic - Works In Both Anabolic & Catabolic Pathways |
32:06 | |
| |
| Biosynthetic Processes |
34:29 | |
| |
| Anaplerotic Reactions Overview |
37:26 | |
| |
| Anaplerotic: Reaction 1 |
41:42 | |
Section 11: Catabolism of Fatty Acids |
|
Fatty Acid Catabolism I |
48:11 |
| |
Intro |
0:00 | |
| |
Introduction to Fatty Acid Catabolism |
0:21 | |
| |
| Introduction to Fatty Acid Catabolism |
0:22 | |
| |
Vertebrate Cells Obtain Fatty Acids for Catabolism From 3 Sources |
2:16 | |
| |
| Diet: Part 1 |
4:00 | |
| |
| Diet: Part 2 |
5:35 | |
| |
| Diet: Part 3 |
6:20 | |
| |
| Diet: Part 4 |
6:47 | |
| |
| Diet: Part 5 |
10:18 | |
| |
| Diet: Part 6 |
10:54 | |
| |
| Diet: Part 7 |
12:04 | |
| |
| Diet: Part 8 |
12:26 | |
| |
| Fats Stored in Adipocytes Overview |
13:54 | |
| |
| Fats Stored in Adipocytes (Fat Cells): Part 1 |
16:13 | |
| |
| Fats Stored in Adipocytes (Fat Cells): Part 2 |
17:16 | |
| |
| Fats Stored in Adipocytes (Fat Cells): Part 3 |
19:42 | |
| |
| Fats Stored in Adipocytes (Fat Cells): Part 4 |
20:52 | |
| |
| Fats Stored in Adipocytes (Fat Cells): Part 5 |
22:56 | |
| |
Mobilization of TAGs Stored in Fat Cells |
24:35 | |
| |
Fatty Acid Oxidation |
28:29 | |
| |
| Fatty Acid Oxidation |
28:48 | |
| |
| 3 Reactions of the Carnitine Shuttle |
30:42 | |
| |
| Carnitine Shuttle & The Mitochondrial Matrix |
36:25 | |
| |
| CAT I |
43:58 | |
| |
| Carnitine Shuttle is the Rate-Limiting Steps |
46:24 | |
|
Fatty Acid Catabolism II |
45:58 |
| |
Intro |
0:00 | |
| |
Fatty Acid Catabolism |
0:15 | |
| |
| Fatty Acid Oxidation Takes Place in 3 Stages |
0:16 | |
| |
β-Oxidation |
2:05 | |
| |
| β-Oxidation Overview |
2:06 | |
| |
| Reaction 1 |
4:20 | |
| |
| Reaction 2 |
7:35 | |
| |
| Reaction 3 |
8:52 | |
| |
| Reaction 4 |
10:16 | |
| |
| β-Oxidation Reactions Discussion |
11:34 | |
| |
Notes On β-Oxidation |
15:14 | |
| |
| Double Bond After The First Reaction |
15:15 | |
| |
| Reaction 1 is Catalyzed by 3 Isozymes of Acyl-CoA Dehydrogenase |
16:04 | |
| |
| Reaction 2 & The Addition of H₂O |
18:38 | |
| |
| After Reaction 4 |
19:24 | |
| |
| Production of ATP |
20:04 | |
| |
β-Oxidation of Unsaturated Fatty Acid |
21:25 | |
| |
| β-Oxidation of Unsaturated Fatty Acid |
22:36 | |
| |
β-Oxidation of Mono-Unsaturates |
24:49 | |
| |
| β-Oxidation of Mono-Unsaturates: Reaction 1 |
24:50 | |
| |
| β-Oxidation of Mono-Unsaturates: Reaction 2 |
28:43 | |
| |
| β-Oxidation of Mono-Unsaturates: Reaction 3 |
30:50 | |
| |
| β-Oxidation of Mono-Unsaturates: Reaction 4 |
31:06 | |
| |
β-Oxidation of Polyunsaturates |
32:29 | |
| |
| β-Oxidation of Polyunsaturates: Part 1 |
32:30 | |
| |
| β-Oxidation of Polyunsaturates: Part 2 |
37:08 | |
| |
| β-Oxidation of Polyunsaturates: Part 3 |
40:25 | |
|
Fatty Acid Catabolism III |
33:18 |
| |
Intro |
0:00 | |
| |
Fatty Acid Catabolism |
0:43 | |
| |
| Oxidation of Fatty Acids With an Odd Number of Carbons |
0:44 | |
| |
| β-oxidation in the Mitochondrion & Two Other Pathways |
9:08 | |
| |
| ω-oxidation |
10:37 | |
| |
| α-oxidation |
17:22 | |
| |
Ketone Bodies |
19:08 | |
| |
| Two Fates of Acetyl-CoA Formed by β-Oxidation Overview |
19:09 | |
| |
| Ketone Bodies: Acetone |
20:42 | |
| |
| Ketone Bodies: Acetoacetate |
20:57 | |
| |
| Ketone Bodies: D-β-hydroxybutyrate |
21:25 | |
| |
| Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 1 |
22:05 | |
| |
| Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 2 |
26:59 | |
| |
| Two Fates of Acetyl-CoA Formed by β-Oxidation: Part 3 |
30:52 | |
Section 12: Catabolism of Amino Acids and the Urea Cycle |
|
Overview & The Aminotransferase Reaction |
40:59 |
| |
Intro |
0:00 | |
| |
Overview of The Aminotransferase Reaction |
0:25 | |
| |
| Overview of The Aminotransferase Reaction |
0:26 | |
| |
| The Aminotransferase Reaction: Process 1 |
3:06 | |
| |
| The Aminotransferase Reaction: Process 2 |
6:46 | |
| |
| Alanine From Muscle Tissue |
10:54 | |
| |
| Bigger Picture of the Aminotransferase Reaction |
14:52 | |
| |
| Looking Closely at Process 1 |
19:04 | |
| |
| Pyridoxal Phosphate (PLP) |
24:32 | |
| |
| Pyridoxamine Phosphate |
25:29 | |
| |
| Pyridoxine (B6) |
26:38 | |
| |
| The Function of PLP |
27:12 | |
| |
| Mechanism Examples |
28:46 | |
| |
| Reverse Reaction: Glutamate to α-Ketoglutarate |
35:34 | |
|
Glutamine & Alanine: The Urea Cycle I |
39:18 |
| |
Intro |
0:00 | |
| |
Glutamine & Alanine: The Urea Cycle I |
0:45 | |
| |
| Excess Ammonia, Glutamate, and Glutamine |
0:46 | |
| |
| Glucose-Alanine Cycle |
9:54 | |
| |
| Introduction to the Urea Cycle |
20:56 | |
| |
| The Urea Cycle: Production of the Carbamoyl Phosphate |
22:59 | |
| |
| The Urea Cycle: Reaction & Mechanism Involving the Carbamoyl Phosphate Synthetase |
33:36 | |
|
Glutamine & Alanine: The Urea Cycle II |
36:21 |
| |
Intro |
0:00 | |
| |
Glutamine & Alanine: The Urea Cycle II |
0:14 | |
| |
| The Urea Cycle Overview |
0:34 | |
| |
| Reaction 1: Ornithine → Citrulline |
7:30 | |
| |
| Reaction 2: Citrulline → Citrullyl-AMP |
11:15 | |
| |
| Reaction 2': Citrullyl-AMP → Argininosuccinate |
15:25 | |
| |
| Reaction 3: Argininosuccinate → Arginine |
20:42 | |
| |
| Reaction 4: Arginine → Orthinine |
24:00 | |
| |
| Links Between the Citric Acid Cycle & the Urea Cycle |
27:47 | |
| |
| Aspartate-argininosuccinate Shunt |
32:36 | |
|
Amino Acid Catabolism |
47:58 |
| |
Intro |
0:00 | |
| |
Amino Acid Catabolism |
0:10 | |
| |
| Common Amino Acids and 6 Major Products |
0:11 | |
| |
| Ketogenic Amino Acid |
1:52 | |
| |
| Glucogenic Amino Acid |
2:51 | |
| |
| Amino Acid Catabolism Diagram |
4:18 | |
| |
| Cofactors That Play a Role in Amino Acid Catabolism |
7:00 | |
| |
| Biotin |
8:42 | |
| |
| Tetrahydrofolate |
10:44 | |
| |
| S-Adenosylmethionine (AdoMet) |
12:46 | |
| |
| Tetrahydrobiopterin |
13:53 | |
| |
| S-Adenosylmethionine & Tetrahydrobiopterin Molecules |
14:41 | |
| |
Catabolism of Phenylalanine |
18:30 | |
| |
| Reaction 1: Phenylalanine to Tyrosine |
18:31 | |
| |
| Reaction 2: Tyrosine to p-Hydroxyphenylpyruvate |
21:36 | |
| |
| Reaction 3: p-Hydroxyphenylpyruvate to Homogentisate |
23:50 | |
| |
| Reaction 4: Homogentisate to Maleylacetoacetate |
25:42 | |
| |
| Reaction 5: Maleylacetoacetate to Fumarylacetoacetate |
28:20 | |
| |
| Reaction 6: Fumarylacetoacetate to Fumarate & Succinyl-CoA |
29:51 | |
| |
| Reaction 7: Fate of Fumarate & Succinyl-CoA |
31:14 | |
| |
Phenylalanine Hydroxylase |
33:33 | |
| |
| The Phenylalanine Hydroxylase Reaction |
33:34 | |
| |
| Mixed-Function Oxidases |
40:26 | |
| |
| When Phenylalanine Hydoxylase is Defective: Phenylketonuria (PKU) |
44:13 | |
Section 13: Oxidative Phosphorylation and ATP Synthesis |
|
Oxidative Phosphorylation I |
41:11 |
| |
Intro |
0:00 | |
| |
Oxidative Phosphorylation |
0:54 | |
| |
| Oxidative Phosphorylation Overview |
0:55 | |
| |
| Mitochondrial Electron Transport Chain Diagram |
7:15 | |
| |
| Enzyme Complex I of the Electron Transport Chain |
12:27 | |
| |
| Enzyme Complex II of the Electron Transport Chain |
14:02 | |
| |
| Enzyme Complex III of the Electron Transport Chain |
14:34 | |
| |
| Enzyme Complex IV of the Electron Transport Chain |
15:30 | |
| |
| Complexes Diagram |
16:25 | |
| |
Complex I |
18:25 | |
| |
| Complex I Overview |
18:26 | |
| |
| What is Ubiquinone or Coenzyme Q? |
20:02 | |
| |
| Coenzyme Q Transformation |
22:37 | |
| |
| Complex I Diagram |
24:47 | |
| |
| Fe-S Proteins |
26:42 | |
| |
| Transfer of H⁺ |
29:42 | |
| |
Complex II |
31:06 | |
| |
| Succinate Dehydrogenase |
31:07 | |
| |
| Complex II Diagram & Process |
32:54 | |
| |
| Other Substrates Pass Their e⁻ to Q: Glycerol 3-Phosphate |
37:31 | |
| |
| Other Substrates Pass Their e⁻ to Q: Fatty Acyl-CoA |
39:02 | |
|
Oxidative Phosphorylation II |
36:27 |
| |
Intro |
0:00 | |
| |
Complex III |
0:19 | |
| |
| Complex III Overview |
0:20 | |
| |
| Complex III: Step 1 |
1:56 | |
| |
| Complex III: Step 2 |
6:14 | |
| |
Complex IV |
8:42 | |
| |
| Complex IV: Cytochrome Oxidase |
8:43 | |
| |
Oxidative Phosphorylation, cont'd |
17:18 | |
| |
| Oxidative Phosphorylation: Summary |
17:19 | |
| |
| Equation 1 |
19:13 | |
| |
| 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 Pump |
28:48 | |
| |
| Free Energy Change in Active Mitochondria |
32:02 | |