Biochemistry, the chemistry of biological molecules, explains the complex processes that sustain all living organisms. This college-level course taught by Professor Raffi Hovasapian is perfect for Pre-Medical students as well as Biology and Chemistry majors. Each lesson contains fundamental definitions, numerous worked-out examples, and many step-by-step explanations of complex processes. Professor Hovasapian carefully goes through how Proteins, Carbohydrates, Nucleic Acids and other biomolecules make life on Earth possible. Combining his triple degrees in Mathematics, Chemistry, and Classics, along with 10+ years of teaching experience, Professor Hovasapian expertly helps students understand difficult biochemical concepts. Raffi also teaches AP Chemistry, Multivariable Calculus, and Linear Algebra on Educator.
| I. Preliminaries on Aqueous Chemistry |
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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 | |
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| Covalent Compounds |
6:55 | |
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| Ionic Compounds |
7:39 | |
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| Example: Table Sugar |
9:12 | |
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| Example: MgCl₂ |
10:40 | |
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| Expressing Concentration: Molarity |
13:42 | |
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Example 1 |
14:47 | |
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| Example 1: Question |
14:50 | |
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| Example 1: Solution |
15:40 | |
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| 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 | |
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Example 3 |
29:30 | |
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| Example 3: Question |
29:31 | |
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| Example 3: Solution |
31:02 | |
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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 | |
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| Example 2: Alternative Approach |
12:05 | |
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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 | |
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| Osmotic Pressure: Conceptual Example |
24:00 | |
| | |
| Equation for Osmotic Pressure |
29:30 | |
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| Example of 'i' |
31:38 | |
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| Example 3 |
32:50 | |
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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 | |
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| Example 2: Osmolarity |
15:19 | |
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| Isotonic, Hypertonic, and Hypotonic |
20:20 | |
| | |
| Example 3 |
22:20 | |
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| More on Isotonic, Hypertonic, and Hypotonic |
26:14 | |
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| 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 | |
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| Example 1 |
6:39 | |
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| pH |
9:43 | |
| | |
| Strong Acids |
11:10 | |
| | |
| Strong Bases |
13:52 | |
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| Weak Acids & Bases Overview |
14:32 | |
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| Weak Acids |
15:49 | |
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| Example 2: Phosphoric Acid |
19:30 | |
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| 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 | |
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| 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 | |
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| Example 1: Part B |
4:40 | |
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Example 2 |
9:02 | |
| | |
| Example 2: Question |
9:03 | |
| | |
| 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 | |
| | |
| Example 3: pH After |
24:24 | |
| | |
| Example 3: New pH |
27:54 | |
| | |
Example 4 |
30:00 | |
| | |
| Example 4: Question |
30:01 | |
| | |
| Example 4: Equilibria |
32:52 | |
| | |
| Example 4: 1st Reaction |
38:04 | |
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| 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 | |
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| Example 4: Formation & Hydrolysis of a Peptide Bond Between the Amino Acids Alanine & Serine |
14:56 | |
| II. 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 | |
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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 | |
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Sequencing Larger Peptides & Proteins |
62:33 |
| | |
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 | |
| III. 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 | |
| IV. 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 |
63:36 |
| | |
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 |
67:16 |
| | |
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 | |
| V. 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 | |
| VI. Carbohydrates |
| |
Monosaccharides |
77:46 |
| | |
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 | |
| VII. 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 | |
| VIII. 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 | |
| IX. 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 |
61:47 |
| | |
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 | |
| X. 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 | |
| XI. 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 | |
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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 | |
| XII. 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 | |
| XIII. 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 | |