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Dr. Carleen Eaton

Dr. Carleen Eaton

Enzymes

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Table of Contents

Section 1: Chemistry of Life
Elements, Compounds, and Chemical Bonds

56m 18s

Intro
0:00
Elements
0:09
Elements
0:48
Matter
0:55
Naturally Occurring Elements
1:12
Atomic Number and Atomic Mass
2:39
Compounds
3:06
Molecule
3:07
Compounds
3:14
Examples
3:20
Atoms
4:53
Atoms
4:56
Protons, Neutrons, and Electrons
5:29
Isotopes
10:42
Energy Levels of Electrons
13:01
Electron Shells
13:13
Valence Shell
13:22
Example: Electron Shells and Potential Energy
13:28
Covalent Bonds
19:52
Covalent Bonds
19:54
Examples
20:03
Polar and Nonpolar Covalent Bonds
23:54
Polar Bond
24:07
Nonpolar Bonds
24:17
Examples
24:25
Ionic Bonds
29:04
Ionic Bond, Cations, Anions
29:19
Example: NaCl
29:30
Hydrogen Bond
33:18
Hydrogen Bond
33:20
Chemical Reactions
35:36
Example: Reactants, Products and Chemical Reactions
35:45
Molecular Mass and Molar Concentration
38:45
Avogadro's Number and Mol
39:12
Examples: Molecular Mass and Molarity
42:10
Example 1: Proton, Neutrons and Electrons
47:05
Example 2: Reactants and Products
49:35
Example 3: Bonding
52:39
Example 4: Mass
53:59
Properties of Water

50m 23s

Intro
0:00
Molecular Structure of Water
0:21
Molecular Structure of Water
0:27
Properties of Water
4:30
Cohesive
4:55
Transpiration
5:29
Adhesion
6:20
Surface Tension
7:17
Properties of Water, cont.
9:14
Specific Heat
9:25
High Heat Capacity
13:24
High Heat of Evaporation
16:42
Water as a Solvent
21:13
Solution
21:28
Solvent
21:48
Example: Water as a Solvent
22:22
Acids and Bases
25:40
Example
25:41
pH
36:30
pH Scale: Acidic, Neutral, and Basic
36:35
Example 1: Molecular Structure and Properties of Water
41:18
Example 2: Special Properties of Water
42:53
Example 3: pH Scale
44:46
Example 4: Acids and Bases
46:19
Organic Compounds

53m 54s

Intro
0:00
Organic Compounds
0:09
Organic Compounds
0:11
Inorganic Compounds
0:15
Examples: Organic Compounds
1:15
Isomers
5:52
Isomers
5:55
Structural Isomers
6:23
Geometric Isomers
8:14
Enantiomers
9:55
Functional Groups
12:46
Examples: Functional Groups
12:59
Amino Group
13:51
Carboxyl Group
14:38
Hydroxyl Group
15:22
Methyl Group
16:14
Carbonyl Group
16:30
Phosphate Group
17:51
Carbohydrates
18:26
Carbohydrates
19:07
Example: Monosaccharides
21:12
Carbohydrates, cont.
24:11
Disaccharides, Polysaccharides and Examples
24:21
Lipids
35:52
Examples of Lipids
36:04
Saturated and Unsaturated
38:57
Phospholipids
43:26
Phospholipids
43:29
Example
43:34
Steroids
46:24
Cholesterol
46:28
Example 1: Isomers
48:11
Example 2: Functional Groups
50:45
Example 3: Galactose, Ketose, and Aldehyde Sugar
52:24
Example 4: Class of Molecules
53:06
Nucleic Acids and Proteins

37m 23s

Intro
0:00
Nucleic Acids
0:09
Deoxyribonucleic Acid (DNA) and Ribonucleic Acid (RNA)
0:29
Nucleic Acids, cont.
2:56
Purines
3:10
Pyrimidines
3:32
Double Helix
4:59
Double Helix and Example
5:01
Proteins
12:33
Amino Acids and Polypeptides
12:39
Examples: Amino Acid
13:25
Polypeptide Formation
18:09
Peptide Bonds
18:14
Primary Structure
18:35
Protein Structure
23:19
Secondary Structure
23:22
Alpha Helices and Beta Pleated Sheets
23:34
Protein Structure
25:43
Tertiary Structure
25:44
5 Types of Interaction
26:56
Example 1: Complementary DNA Strand
31:45
Example 2: Differences Between DNA and RNA
33:19
Example 3: Amino Acids
34:32
Example 4: Tertiary Structure of Protein
35:46
Section 2: Cell Structure and Function
Cell Types (Prokaryotic and Eukaryotic)

45m 50s

Intro
0:00
Cell Theory and Cell Types
0:12
Cell Theory
0:13
Prokaryotic and Eukaryotic Cells
0:36
Endosymbiotic Theory
1:13
Study of Cells
4:07
Tools and Techniques
4:08
Light Microscopes
5:08
Light vs. Electron Microscopes: Magnification
5:18
Light vs. Electron Microscopes: Resolution
6:26
Light vs. Electron Microscopes: Specimens
7:53
Electron Microscopes: Transmission and Scanning
8:28
Cell Fractionation
10:01
Cell Fractionation Step 1: Homogenization
10:33
Cell Fractionation Step 2: Spin
11:24
Cell Fractionation Step 3: Differential Centrifugation
11:53
Comparison of Prokaryotic and Eukaryotic Cells
14:12
Prokaryotic vs. Eukaryotic Cells: Domains
14:43
Prokaryotic vs. Eukaryotic Cells: Plasma Membrane
15:40
Prokaryotic vs. Eukaryotic Cells: Cell Walls
16:15
Prokaryotic vs. Eukaryotic Cells: Genetic Materials
16:38
Prokaryotic vs. Eukaryotic Cells: Structures
17:28
Prokaryotic vs. Eukaryotic Cells: Unicellular and Multicellular
18:19
Prokaryotic vs. Eukaryotic Cells: Size
18:31
Plasmids
18:52
Prokaryotic vs. Eukaryotic Cells
19:22
Nucleus
19:24
Organelles
19:48
Cytoskeleton
20:02
Cell Wall
20:35
Ribosomes
20:57
Size
21:37
Comparison of Plant and Animal Cells
22:15
Plasma Membrane
22:55
Plant Cells Only: Cell Walls
23:12
Plant Cells Only: Central Vacuole
25:08
Animal Cells Only: Centrioles
26:40
Animal Cells Only: Lysosomes
27:43
Plant vs. Animal Cells
29:16
Overview of Plant and Animal Cells
29:17
Evidence for the Endosymbiotic Theory
30:52
Characteristics of Mitochondria and Chloroplasts
30:54
Example 1: Prokaryotic vs. Eukaryotic Cells
35:44
Example 2: Endosymbiotic Theory and Evidence
38:38
Example 3: Plant and Animal Cells
41:49
Example 4: Cell Fractionation
43:44
Subcellular Structure

59m 38s

Intro
0:00
Prokaryotic Cells
0:09
Shapes of Prokaryotic Cells
0:22
Cell Wall
1:19
Capsule
3:23
Pili/Fimbria
3:54
Flagella
4:35
Nucleoid
6:16
Plasmid
6:37
Ribosomes
7:09
Eukaryotic Cells (Animal Cell Structure)
8:01
Plasma Membrane
8:13
Microvilli
8:48
Nucleus
9:47
Nucleolus
11:06
Ribosomes: Free and Bound
12:26
Rough Endoplasmic Reticulum (RER)
13:43
Eukaryotic Cells (Animal Cell Structure), cont.
14:51
Endoplasmic Reticulum: Smooth and Rough
15:08
Golgi Apparatus
17:55
Vacuole
20:43
Lysosome
22:01
Mitochondria
25:40
Peroxisomes
28:18
Cytoskeleton
30:41
Cytoplasm and Cytosol
30:53
Microtubules: Centrioles, Spindel Fibers, Clagell, Cillia
32:06
Microfilaments
36:39
Intermediate Filaments and Kerotin
38:52
Eukaryotic Cells (Plant Cell Structure)
40:08
Plasma Membrane, Primary Cell Wall, and Secondary Cell Wall
40:30
Middle Lamella
43:21
Central Cauole
44:12
Plastids: Leucoplasts, Chromoplasts, Chrloroplasts
45:35
Chloroplasts
47:06
Example 1: Structures and Functions
48:46
Example 2: Cell Walls
51:19
Example 3: Cytoskeleton
52:53
Example 4: Antibiotics and the Endosymbiosis Theory
56:55
Cell Membranes and Transport

53m 10s

Intro
0:00
Cell Membrane Structure
0:09
Phospholipids Bilayer
0:11
Chemical Structure: Amphipathic and Fatty Acids
0:25
Cell Membrane Proteins
2:44
Fluid Mosaic Model
2:45
Peripheral Proteins and Integral Proteins
3:19
Transmembrane Proteins
4:34
Cholesterol
4:48
Functions of Membrane Proteins
6:39
Transport Across Cell Membranes
9:52
Transport Across Cell Membranes
9:53
Methods of Passive Transport
12:07
Passive and Active Transport
12:08
Simple Diffusion
12:45
Facilitated Diffusion
15:20
Osmosis
17:17
Definition and Example of Osmosis
17:18
Hypertonic, Hypotonic, and Isotonic
21:47
Active Transport
27:57
Active Transport
28:17
Sodium and Potassium Pump
29:45
Cotransport
34:38
2 Types of Active Transport
37:09
Endocytosis and Exocytosis
37:38
Endocytosis and Exocytosis
37:51
Types of Endocytosis: Pinocytosis
40:39
Types of Endocytosis: Phagocytosis
41:02
Receptor Mediated Endocytosis
41:27
Receptor Mediated Endocytosis
41:28
Example 1: Cell Membrane and Permeable Substances
43:59
Example 2: Osmosis
45:20
Example 3: Active Transport, Cotransport, Simple and Facilitated Diffusion
47:36
Example 4: Match Terms with Definition
50:55
Cellular Communication

57m 9s

Intro
0:00
Extracellular Matrix
0:28
The Extracellular Matrix (ECM)
0:29
ECM in Animal Cells
0:55
Fibronectin and Integrins
1:34
Intercellular Communication in Plants
2:48
Intercellular Communication in Plants: Plasmodesmata
2:50
Cell to Cell Communication in Animal Cells
3:39
Cell Junctions
3:42
Desmosomes
3:54
Tight Junctions
5:07
Gap Junctions
7:00
Cell Signaling
8:17
Cell Signaling: Ligand and Signal Transduction Pathway
8:18
Direct Contact
8:48
Over Distances Contact and Hormones
10:09
Stages of Cell Signaling
11:53
Reception Phase
11:54
Transduction Phase
13:49
Response Phase
14:45
Cell Membrane Receptors
15:37
G-Protein Coupled Receptor
15:38
Cell Membrane Receptor, Cont.
21:37
Receptor Tyrosine Kinases (RTKs)
21:38
Autophosphorylation, Monomer, and Dimer
22:57
Cell Membrane Receptor, Cont.
27:01
Ligand-Gated Ion Channels
27:02
Intracellular Receptors
29:43
Intracellular Receptor and Receptor -Ligand Complex
29:44
Signal Transduction
32:57
Signal Transduction Pathways
32:58
Adenylyl Cyclase and cAMP
35:53
Second Messengers
39:18
cGMP, Inositol Trisphosphate, and Diacylglycerol
39:20
Cell Response
45:15
Cell Response
45:16
Apoptosis
46:57
Example 1: Tight Junction and Gap Junction
48:29
Example 2: Three Phases of Cell Signaling
51:48
Example 3: Ligands and Binding of Hormone
54:03
Example 4: Signal Transduction
56:06
Section 3: Cell Division
The Cell Cycle

37m 49s

Intro
0:00
Functions of Cell Division
0:09
Overview of Cell Division: Reproduction, Growth, and Repair
0:11
Important Term: Daughter Cells
2:25
Chromosome Structure
3:36
Chromosome Structure: Sister Chromatids and Centromere
3:37
Chromosome Structure: Chromatin
4:31
Chromosome with One Chromatid or Two Chromatids
5:25
Chromosome Structure: Long and Short Arm
6:49
Mitosis and Meiosis
7:00
Mitosis
7:41
Meiosis
8:40
The Cell Cycle
10:43
Mitotic Phase and Interphase
10:44
Cytokinesis
15:51
Cytokinesis in Animal Cell: Cleavage Furrow
15:52
Cytokinesis in Plant Cell: Cell Plate
17:28
Control of the Cell Cycle
18:28
Cell Cycle Control System and Checkpoints
18:29
Cyclins and Cyclin Dependent Kinases
21:18
Cyclins and Cyclin Dependent Kinases (CDKSs)
21:20
MPF
23:17
Internal Factor Regulating Cell Cycle
24:00
External Factor Regulating Cell Cycle
24:53
Contact Inhibition and Anchorage Dependent
25:53
Cancer and the Cell Cycle
27:42
Cancer Cells
27:46
Example1: Parts of the Chromosome
30:15
Example 2: Cell Cycle
31:50
Example 3: Control of the Cell Cycle
33:32
Example 4: Cancer and the Cell
35:01
Mitosis

35m 1s

Intro
0:00
Review of the Cell Cycle
0:09
Interphase: G1 Phase
0:34
Interphase: S Phase
0:56
Interphase: G2 Phase
1:31
M Phase: Mitosis and Cytokinesis
1:47
Overview of Mitosis
3:08
What is Mitosis?
3:10
Overview of Mitosis
3:17
Diploid and Haploid
5:37
Homologous Chromosomes
6:04
The Spindle Apparatus
11:57
The Spindle Apparatus
12:00
Centrosomes and Centrioles
12:40
Microtubule Organizing Center
13:03
Spindle Fiber of Spindle Microtubules
13:23
Kinetochores
14:06
Asters
15:45
Prophase
16:47
First Phase of Mitosis: Prophase
16:54
Metaphase
20:05
Second Phase of Mitosis: Metaphase
20:10
Anaphase
22:52
Third Phase of Mitosis: Anaphase
22:53
Telophase and Cytokinesis
24:34
Last Phase of Mitosis: Telophase and Cytokinesis
24:35
Summary of Mitosis
27:46
Summary of Mitosis
27:47
Example 1: Spindle Apparatus
28:50
Example 2: Last Phase of Mitosis
30:39
Example 3: Prophase
32:41
Example 4: Identify the Phase
33:52
Meiosis

1h 58s

Intro
0:00
Haploid and Diploid Cells
0:09
Diploid and Somatic Cells
0:29
Haploid and Gametes
1:20
Example: Human Cells and Chromosomes
1:41
Sex Chromosomes
6:00
Comparison of Mitosis and Meiosis
10:42
Mitosis Vs. Meiosis: Cell Division
10:59
Mitosis Vs. Meiosis: Daughter Cells
12:31
Meiosis: Pairing of Homologous Chromosomes
13:40
Mitosis and Meiosis
14:21
Process of Mitosis
14:27
Process of Meiosis
16:12
Synapsis and Crossing Over
19:14
Prophase I: Synapsis and Crossing Over
19:15
Chiasmata
22:33
Meiosis I
25:49
Prophase I: Crossing Over
25:50
Metaphase I: Homologs Line Up
26:00
Anaphase I: Homologs Separate
28:16
Telophase I and Cytokinesis
29:15
Independent Assortment
30:58
Meiosis II
32:17
Propphase II
33:50
Metaphase II
34:06
Anaphase II
34:50
Telophase II
36:09
Cytokinesis
37:00
Summary of Meiosis
38:15
Summary of Meiosis
38:16
Cell Division Mechanism in Plants
41:57
Example 1: Cell Division and Meiosis
46:15
Example 2: Phases of Meiosis
50:22
Example 3: Label the Figure
54:29
Example 4: Four Differences Between Mitosis and Meiosis
56:37
Section 4: Cellular Energetics
Enzymes

51m 3s

Intro
0:00
Law of Thermodynamics
0:08
Thermodynamics
0:09
The First Law of Thermodynamics
0:37
The Second Law of Thermodynamics
1:24
Entropy
1:35
The Gibbs Free Energy Equation
3:07
The Gibbs Free Energy Equation
3:08
ATP
8:23
Adenosine Triphosphate (ATP)
8:24
Cellular Respiration
11:32
Catabolic Pathways
12:28
Anabolic Pathways
12:54
Enzymes
14:31
Enzymes
14:32
Enzymes and Exergonic Reaction
14:40
Enzymes and Endergonic Reaction
16:36
Enzyme Specificity
21:29
Substrate
21:41
Induced Fit
23:04
Factors Affecting Enzyme Activity
25:55
Substrate Concentration
26:07
pH
27:10
Temperature
29:14
Presence of Cofactors
29:57
Regulation of Enzyme Activity
31:12
Competitive Inhibitors
32:13
Noncompetitive Inhibitors
33:52
Feedback Inhibition
35:22
Allosteric Interactions
36:56
Allosteric Regulators
37:00
Example 1: Is the Inhibitor Competitive or Noncompetitive?
40:49
Example 2: Thermophiles
44:18
Example 3: Exergonic or Endergonic
46:09
Example 4: Energy Vs. Reaction Progress Graph
48:47
Glycolysis and Anaerobic Respiration

38m 1s

Intro
0:00
Cellular Respiration Overview
0:13
Cellular Respiration
0:14
Anaerobic Respiration vs. Aerobic Respiration
3:50
Glycolysis Overview
4:48
Overview of Glycolysis
4:50
Glycolysis Involves a Redox Reaction
7:02
Redox Reaction
7:04
Glycolysis
15:04
Important Facts About Glycolysis
15:07
Energy Invested Phase
16:12
Splitting of Fructose 1,6-Phosphate and Energy Payoff Phase
17:50
Substrate Level Phophorylation
22:12
Aerobic Versus Anaerobic Respiration
23:57
Aerobic Versus Anaerobic Respiration
23:58
Cellular Respiration Overview
27:15
When Cellular Respiration is Anaerobic
27:17
Glycolysis
28:26
Alcohol Fermentation
28:45
Lactic Acid Fermentation
29:58
Example 1: Glycolysis
31:04
Example 2: Glycolysis, Fermentation and Anaerobic Respiration
33:44
Example 3: Aerobic Respiration Vs. Anaerobic Respiration
35:25
Example 4: Exergonic Reaction and Endergonic Reaction
36:42
Aerobic Respiration

51m 6s

Intro
0:00
Aerobic Vs. Anaerobic Respiration
0:06
Aerobic and Anaerobic Comparison
0:07
Review of Glycolysis
1:48
Overview of Glycolysis
2:06
Glycolysis: Energy Investment Phase
2:25
Glycolysis: Energy Payoff Phase
2:58
Conversion of Pyruvate to Acetyl CoA
4:55
Conversion of Pyruvate to Acetyl CoA
4:56
Energy Formation
8:06
Mitochondrial Structure
8:58
Endosymbiosis Theory
9:23
Matrix
10:00
Outer Membrane, Inner Membrane, and Intermembrane Space
10:43
Cristae
11:47
The Citric Acid Cycle
12:11
The Citric Acid Cycle (Also Called Krebs Cycle)
12:12
Substrate Level Phosphorylation
18:47
Summary of ATP, NADH, and FADH2 Production
23:13
Process: Glycolysis
23:28
Process: Acetyl CoA Production
23:36
Process: Citric Acid Cycle
23:52
The Electron Transport Chain
24:24
Oxidative Phosphorylation
24:28
The Electron Transport Chain and ATP Synthase
25:20
Carrier Molecules: Cytochromes
27:18
Carrier Molecules: Flavin Mononucleotide (FMN)
28:05
Chemiosmosis
32:46
The Process of Chemiosmosis
32:47
Summary of ATP Produced by Aerobic Respiration
38:24
ATP Produced by Aerobic Respiration
38:27
Example 1: Aerobic Respiration
43:38
Example 2: Label the Location for Each Process and Structure
45:08
Example 3: The Electron Transport Chain
47:06
Example 4: Mitochondrial Inner Membrane
48:38
Photosynthesis

1h 2m 52s

Intro
0:00
Photosynthesis
0:09
Introduction to Photosynthesis
0:10
Autotrophs and Heterotrophs
0:25
Overview of Photosynthesis Reaction
1:05
Leaf Anatomy and Chloroplast Structure
2:54
Chloroplast
2:55
Cuticle
3:16
Upper Epidermis
3:27
Mesophyll
3:40
Stomates
4:00
Guard Cells
4:45
Transpiration
5:01
Vascular Bundle
5:20
Stroma and Double Membrane
6:20
Grana
7:17
Thylakoids
7:30
Dark Reaction and Light Reaction
7:46
Light Reactions
8:43
Light Reactions
8:47
Pigments: Chlorophyll a, Chlorophyll b, and Carotenoids
9:19
Wave and Particle
12:10
Photon
12:34
Photosystems
13:24
Photosystems
13:28
Reaction-Center Complex and Light Harvesting Complexes
14:01
Noncyclic Photophosphorylation
17:46
Noncyclic Photophosphorylation Overview
17:47
What is Photophosphorylation?
18:25
Noncyclic Photophosphorylation Process
19:07
Photolysis and The Rest of Noncyclic Photophosphorylation
21:33
Cyclic Photophosphorylation
31:45
Cyclic Photophosphorylation
31:46
Light Independent Reactions
34:34
The Calvin Cycle
34:35
C3 Plants and Photorespiration
40:31
C3 Plants and Photorespiration
40:32
C4 Plants
45:32
C4 Plants: Structures and Functions
45:33
CAM Plants
50:25
CAM Plants: Structures and Functions
50:35
Example 1: Calvin Cycle
54:34
Example 2: C4 Plant
55:48
Example 3: Photosynthesis and Photorespiration
58:35
Example 4: CAM Plants
1:00:41
Section 5: Molecular Genetics
DNA Synthesis

38m 45s

Intro
0:00
Review of DNA Structure
0:09
DNA Molecules
0:10
Nitrogenous Base: Pyrimidines and Purines
1:25
DNA Double Helix
3:03
Complementary Strands of DNA
3:12
5' to 3' & Antiparallel
4:55
Overview of DNA Replication
7:10
DNA Replication & Semiconservative
7:11
DNA Replication
10:26
Origin of Replication
10:28
Helicase
11:10
Single-Strand Binding Protein
12:05
Topoisomerases
13:14
DNA Polymerase
14:26
Primase
15:55
Leading and Lagging Strands
16:51
Leading Strand and Lagging Strand
16:52
Okazaki Fragments
18:10
DNA Polymerase I
20:11
Ligase
21:12
Proofreading and Mismatch Repair
22:18
Proofreading
22:19
Mismatch
23:33
Telomeres
24:58
Telomeres
24:59
Example 1: Function of Enzymes During DNA Synthesis
28:09
Example 2: Accuracy of the DNA Sequence
31:42
Example 3: Leading Strand and Lagging Strand
32:38
Example 4: Telomeres
35:40
Transcription and Translation

1h 17m 1s

Intro
0:00
Transcription and Translation Overview
0:07
From DNA to RNA to Protein
0:09
Structure and Types of RNA
3:14
Structure and Types of RNA
3:33
mRNA
6:19
rRNA
7:02
tRNA
7:28
Transcription
7:54
Initiation Phase
8:11
Elongation Phase
12:12
Termination Phase
14:51
RNA Processing
16:11
Types of RNA Processing
16:12
Exons and Introns
16:35
Splicing & Spliceosomes
18:27
Addition of a 5' Cap and a Poly A tail
20:41
Alternative Splicing
21:43
Translation
23:41
Nucleotide Triplets or Codons
23:42
Start Codon
25:24
Stop Codons
25:38
Coding of Amino Acids and Wobble Position
25:57
Translation Cont.
28:29
Transfer RNA (tRNA): Structures and Functions
28:30
Ribosomes
35:15
Peptidyl, Aminoacyl, and Exit Site
35:23
Steps of Translation
36:58
Initiation Phase
37:12
Elongation Phase
43:12
Termination Phase
45:28
Mutations
49:43
Types of Mutations
49:44
Substitutions: Silent
51:11
Substitutions: Missense
55:27
Substitutions: Nonsense
59:37
Insertions and Deletions
1:01:10
Example 1: Three Types of Processing that are Performed on pre-mRNA
1:06:53
Example 2: The Process of Translation
1:09:10
Example 3: Transcription
1:12:04
Example 4: Three Types of Substitution Mutations
1:14:09
Viral Structure and Genetics

43m 12s

Intro
0:00
Structure of Viruses
0:09
Structure of Viruses: Capsid and Envelope
0:10
Bacteriophage
1:48
Other Viruses
2:28
Overview of Viral Reproduction
3:15
Host Range
3:48
Step 1: Bind to Host Cell
4:39
Step 2: Viral Nuclei Acids Enter the Cell
5:15
Step 3: Viral Nucleic Acids & Proteins are Synthesized
5:54
Step 4: Virus Assembles
6:34
Step 5: Virus Exits the Cell
6:55
The Lytic Cycle
7:37
Steps in the Lytic Cycle
7:38
The Lysogenic Cycle
11:27
Temperate Phage
11:34
Steps in the Lysogenic Cycle
12:09
RNA Viruses
16:57
Types of RNA Viruses
17:15
Positive Sense
18:16
Negative Sense
18:48
Reproductive Cycle of RNA Viruses
19:32
Retroviruses
25:48
Complementary DNA (cDNA) & Reverse Transcriptase
25:49
Life Cycle of a Retrovirus
28:22
Prions
32:42
Prions: Definition and Examples
32:45
Viroids
34:46
Example 1: The Lytic Cycle
35:37
Example 2: Retrovirus
38:03
Example 3: Positive Sense RNA vs. Negative Sense RNA
39:10
Example 4: The Lysogenic Cycle
40:42
Bacterial Genetics and Gene Regulation

49m 45s

Intro
0:00
Bacterial Genomes
0:09
Structure of Bacterial Genomes
0:16
Transformation
1:22
Transformation
1:23
Vector
2:49
Transduction
3:32
Process of Transduction
3:38
Conjugation
8:06
Conjugation & F factor
8:07
Operons
14:02
Definition and Example of Operon
14:52
Structural Genes
16:23
Promoter Region
17:04
Regulatory Protein & Operators
17:53
The lac Operon
20:09
The lac Operon: Inducible System
20:10
The trp Operon
28:02
The trp Operon: Repressible System
28:03
Corepressor
31:37
Anabolic & Catabolic
33:12
Positive Regulation of the lac Operon
34:39
Positive Regulation of the lac Operon
34:40
Example 1: The Process of Transformation
39:07
Example 2: Operon & Terms
43:29
Example 3: Inducible lac Operon and Repressible trp Operon
45:15
Example 4: lac Operon
47:10
Eukaryotic Gene Regulation and Mobile Genetic Elements

54m 26s

Intro
0:00
Mechanism of Gene Regulation
0:11
Differential Gene Expression
0:13
Levels of Regulation
2:24
Chromatin Structure and Modification
4:35
Chromatin Structure
4:36
Levels of Packing
5:50
Euchromatin and Heterochromatin
8:58
Modification of Chromatin Structure
9:58
Epigenetic
12:49
Regulation of Transcription
14:20
Promoter Region, Exon, and Intron
14:26
Enhancers: Control Element
15:31
Enhancer & DNA-Bending Protein
17:25
Coordinate Control
21:23
Silencers
23:01
Post-Transcriptional Regulation
24:05
Post-Transcriptional Regulation
24:07
Alternative Splicing
27:19
Differences in mRNA Stability
28:02
Non-Coding RNA Molecules: micro RNA & siRNA
30:01
Regulation of Translation and Post-Translational Modifications
32:31
Regulation of Translation and Post-Translational Modifications
32:55
Ubiquitin
35:21
Proteosomes
36:04
Transposons
37:50
Mobile Genetic Elements
37:56
Barbara McClintock
38:37
Transposons & Retrotransposons
40:38
Insertion Sequences
43:14
Complex Transposons
43:58
Example 1: Four Mechanisms that Decrease Production of Protein
45:13
Example 2: Enhancers and Gene Expression
49:09
Example 3: Primary Transcript
50:41
Example 4: Retroviruses and Retrotransposons
52:11
Biotechnology

49m 26s

Intro
0:00
Definition of Biotechnology
0:08
Biotechnology
0:09
Genetic Engineering
1:05
Example: Golden Corn
1:57
Recombinant DNA
2:41
Recombinant DNA
2:42
Transformation
3:24
Transduction
4:24
Restriction Enzymes, Restriction Sites, & DNA Ligase
5:32
Gene Cloning
13:48
Plasmids
14:20
Gene Cloning: Step 1
17:35
Gene Cloning: Step 2
17:57
Gene Cloning: Step 3
18:53
Gene Cloning: Step 4
19:46
Gel Electrophoresis
27:25
What is Gel Electrophoresis?
27:26
Gel Electrophoresis: Step 1
28:13
Gel Electrophoresis: Step 2
28:24
Gel Electrophoresis: Step 3 & 4
28:39
Gel Electrophoresis: Step 5
29:55
Southern Blotting
31:25
Polymerase Chain Reaction (PCR)
32:11
Polymerase Chain Reaction (PCR)
32:12
Denaturing Phase
35:40
Annealing Phase
36:07
Elongation/ Extension Phase
37:06
DNA Sequencing and the Human Genome Project
39:19
DNA Sequencing and the Human Genome Project
39:20
Example 1: Gene Cloning
40:40
Example 2: Recombinant DNA
43:04
Example 3: Match Terms With Descriptions
45:43
Example 4: Polymerase Chain Reaction
47:36
Section 6: Heredity
Mendelian Genetics

1h 32m 8s

Intro
0:00
Background
0:40
Gregory Mendel & Mendel's Law
0:41
Blending Hypothesis
1:04
Particulate Inheritance
2:08
Terminology
2:55
Gene
3:05
Locus
3:57
Allele
4:37
Dominant Allele
5:48
Recessive Allele
7:38
Genotype
9:22
Phenotype
10:01
Homozygous
10:44
Heterozygous
11:39
Penetrance
11:57
Expressivity
14:15
Mendel's Experiments
15:31
Mendel's Experiments: Pea Plants
15:32
The Law of Segregation
21:16
Mendel's Conclusions
21:17
The Law of Segregation
22:57
Punnett Squares
28:27
Using Punnet Squares
28:30
The Law of Independent Assortment
32:35
Monohybrid
32:38
Dihybrid
33:29
The Law of Independent Assortment
34:00
The Law of Independent Assortment, cont.
38:13
The Law of Independent Assortment: Punnet Squares
38:29
Meiosis and Mendel's Laws
43:38
Meiosis and Mendel's Laws
43:39
Test Crosses
49:07
Test Crosses Example
49:08
Probability: Multiplication Rule and the Addition Rule
53:39
Probability Overview
53:40
Independent Events & Multiplication Rule
55:40
Mutually Exclusive Events & Addition Rule
1:00:25
Incomplete Dominance, Codominance and Multiple Alleles
1:02:55
Incomplete Dominance
1:02:56
Incomplete Dominance, Codominance and Multiple Alleles
1:07:06
Codominance and Multiple Alleles
1:07:08
Polygenic Inheritance and Pleoitropy
1:10:19
Polygenic Inheritance and Pleoitropy
1:10:26
Epistasis
1:12:51
Example of Epistasis
1:12:52
Example 1: Genetic of Eye Color and Height
1:17:39
Example 2: Blood Type
1:21:57
Example 3: Pea Plants
1:25:09
Example 4: Coat Color
1:28:34
Linked Genes and Non-Mendelian Modes of Inheritance

39m 38s

Intro
0:00
Review of the Law of Independent Assortment
0:14
Review of the Law of Independent Assortment
0:24
Linked Genes
6:06
Linked Genes
6:07
Bateson & Pannett: Pea Plants
8:00
Crossing Over and Recombination
15:17
Crossing Over and Recombination
15:18
Extranuclear Genes
20:50
Extranuclear Genes
20:51
Cytoplasmic Genes
21:31
Genomic Imprinting
23:45
Genomic Imprinting
23:58
Methylation
24:43
Example 1: Recombination Frequencies & Linkage Map
27:07
Example 2: Linked Genes
28:39
Example 3: Match Terms to Correct Descriptions
36:46
Example 4: Leber's Optic Neuropathy
38:40
Sex-Linked Traits and Pedigree Analysis

43m 39s

Intro
0:00
Sex-Linked Traits
0:09
Human Chromosomes, XY, and XX
0:10
Thomas Morgan's Drosophila
1:44
X-Inactivation and Barr Bodies
14:48
X-Inactivation Overview
14:49
Calico Cats Example
17:04
Pedigrees
19:24
Definition and Example of Pedigree
19:25
Autosomal Dominant Inheritance
20:51
Example: Huntington's Disease
20:52
Autosomal Recessive Inheritance
23:04
Example: Cystic Fibrosis, Tay-Sachs Disease, and Phenylketonuria
23:05
X-Linked Recessive Inheritance
27:06
Example: Hemophilia, Duchene Muscular Dystrohpy, and Color Blindess
27:07
Example 1: Colorblind
29:48
Example 2: Pedigree
37:07
Example 3: Inheritance Pattern
39:54
Example 4: X-inactivation
41:17
Section 7: Evolution
Natural Selection

1h 3m 28s

Intro
0:00
Background
0:09
Work of Other Scientists
0:15
Aristotle
0:43
Carl Linnaeus
1:32
George Cuvier
2:47
James Hutton
4:10
Thomas Malthus
5:05
Jean-Baptiste Lamark
5:45
Darwin's Theory of Natural Selection
7:50
Evolution
8:00
Natural Selection
8:43
Charles Darwin & The Galapagos Islands
10:20
Genetic Variation
20:37
Mutations
20:38
Independent Assortment
21:04
Crossing Over
24:40
Random Fertilization
25:26
Natural Selection and the Peppered Moth
26:37
Natural Selection and the Peppered Moth
26:38
Types of Natural Selection
29:52
Directional Selection
29:55
Stabilizing Selection
32:43
Disruptive Selection
34:21
Sexual Selection
36:18
Sexual Dimorphism
37:30
Intersexual Selection
37:57
Intrasexual Selection
39:20
Evidence for Evolution
40:55
Paleontology: Fossil Record
41:30
Biogeography
45:35
Continental Drift
46:06
Pangaea
46:28
Marsupials
47:11
Homologous and Analogous Structure
50:10
Homologous Structure
50:12
Analogous Structure
53:21
Example 1: Genetic Variation & Natural Selection
56:15
Example 2: Types of Natural Selection
58:07
Example 3: Mechanisms By Which Genetic Variation is Maintained Within a Population
1:00:12
Example 4: Difference Between Homologous and Analogous Structures
1:01:28
Population Genetic and Evolution

53m 22s

Intro
0:00
Review of Natural Selection
0:12
Review of Natural Selection
0:13
Genetic Drift and Gene Flow
4:40
Definition of Genetic Drift
4:41
Example of Genetic Drift: Cholera Epidemic
5:15
Genetic Drift: Founder Effect
7:28
Genetic Drift: Bottleneck Effect
10:27
Gene Flow
13:00
Quantifying Genetic Variation
14:32
Average Heterozygosity
15:08
Nucleotide Variation
17:05
Maintaining Genetic Variation
18:12
Heterozygote Advantage
19:45
Example of Heterozygote Advantage: Sickle Cell Anemia
20:21
Diploidy
23:44
Geographic Variation
26:54
Frequency Dependent Selection and Outbreeding
28:15
Neutral Traits
30:55
The Hardy-Weinberg Equilibrium
31:11
The Hardy-Weinberg Equilibrium
31:49
The Hardy-Weinberg Conditions
32:42
The Hardy-Weinberg Equation
34:05
The Hardy-Weinberg Example
36:33
Example 1: Match Terms to Descriptions
42:28
Example 2: The Hardy-Weinberg Equilibrium
44:31
Example 3: The Hardy-Weinberg Equilibrium
49:10
Example 4: Maintaining Genetic Variation
51:30
Speciation and Patterns of Evolution

51m 2s

Intro
0:00
Early Life on Earth
0:08
Early Earth
0:09
1920's Oparin & Haldane
0:58
Abiogenesis
2:15
1950's Miller & Urey
2:45
Ribozymes
5:34
3.5 Billion Years Ago
6:39
2.5 Billion Years Ago
7:14
1.5 Billion Years Ago
7:41
Endosymbiosis
8:00
540 Million Years Ago: Cambrian Explosion
9:57
Gradualism and Punctuated Equilibrium
11:46
Gradualism
11:47
Punctuated Equilibrium
12:45
Adaptive Radiation
15:08
Adaptive Radiation
15:09
Example of Adaptive Radiation: Galapogos Islands
17:11
Convergent Evolution, Divergent Evolution, and Coevolution
18:30
Convergent Evolution
18:39
Divergent Evolution
21:30
Coevolution
23:49
Speciation
26:27
Definition and Example of Species
26:29
Reproductive Isolation: Prezygotive
27:49
Reproductive Isolation: Post zygotic
29:28
Allopatric Speciation
30:21
Allopatric Speciation & Geographic Isolation
30:28
Genetic Drift
31:31
Sympatric Speciation
34:10
Sympatric Speciation
34:11
Polyploidy & Autopolyploidy
35:12
Habitat Isolation
39:17
Temporal Isolation
41:27
Selection Selection
41:40
Example 1: Pattern of Evolution
42:53
Example 2: Sympatric Speciation
45:16
Example 3: Patterns of Evolution
48:08
Example 4: Patterns of Evolution
49:27
Section 8: Diversity of Life
Classification

1h 51s

Intro
0:00
Systems of Classification
0:07
Taxonomy
0:08
Phylogeny
1:04
Phylogenetics Tree
1:44
Cladistics
3:37
Classification of Organisms
5:31
Example of Carl Linnaeus System
5:32
Domains
9:26
Kingdoms: Monera, Protista, Plantae, Fungi, Animalia
9:27
Monera
10:06
Phylogentics Tree: Eurkarya, Bacteria, Archaea
11:58
Domain Eukarya
12:50
Domain Bacteria
15:43
Domain Bacteria
15:46
Pathogens
16:41
Decomposers
18:00
Domain Archaea
19:43
Extremophiles Archaea: Thermophiles and Halophiles
19:44
Methanogens
20:58
Phototrophs, Autotrophs, Chemotrophs and Heterotrophs
24:40
Phototrophs and Chemotrophs
25:02
Autotrophs and Heterotrophs
26:54
Photoautotrophs
28:50
Photoheterotrophs
29:28
Chemoautotrophs
30:06
Chemoheterotrophs
31:37
Domain Eukarya
32:40
Domain Eukarya
32:43
Plant Kingdom
34:28
Protists
35:48
Fungi Kingdom
37:06
Animal Kingdom
38:35
Body Symmetry
39:25
Lack Symetry
39:40
Radial Symmetry: Sea Aneome
40:15
Bilateral Symmetry
41:55
Cephalization
43:29
Germ Layers
44:54
Diploblastic Animals
45:18
Triploblastic Animals
45:25
Ectoderm
45:36
Endoderm
46:07
Mesoderm
46:41
Coelomates
47:14
Coelom
47:15
Acoelomate
48:22
Pseudocoelomate
48:59
Coelomate
49:31
Protosomes
50:46
Deuterosomes
51:20
Example 1: Domains
53:01
Example 2: Match Terms with Descriptions
56:00
Example 3: Kingdom Monera and Domain Archaea
57:50
Example 4: System of Classification
59:37
Bacteria

36m 46s

Intro
0:00
Comparison of Domain Archaea and Domain Bacteria
0:08
Overview of Archaea and Bacteria
0:09
Archaea vs. Bacteria: Nucleus, Organelles, and Organization of Genetic Material
1:45
Archaea vs. Bacteria: Cell Walls
2:20
Archaea vs. Bacteria: Number of Types of RNA Pol
2:29
Archaea vs. Bacteria: Membrane Lipids
2:53
Archaea vs. Bacteria: Introns
3:33
Bacteria: Pathogen
4:03
Bacteria: Decomposers and Fix Nitrogen
5:18
Bacteria: Aerobic, Anaerobic, Strict Anaerobes & Facultative Anaerobes
6:02
Phototrophs, Autotrophs, Heterotrophs and Chemotrophs
7:14
Phototrophs and Chemotrophs
7:50
Autotrophs and Heterotrophs
8:53
Photoautotrophs and Photoheterotrophs
10:15
Chemoautotroph and Chemoheterotrophs
11:07
Structure of Bacteria
12:21
Shapes: Cocci, Bacilli, Vibrio, and Spirochetes
12:26
Structures: Plasma Membrane and Cell Wall
14:23
Structures: Nucleoid Region, Plasmid, and Capsule Basal Apparatus, and Filament
15:30
Structures: Flagella, Basal Apparatus, Hook, and Filament
16:36
Structures: Pili, Fimbrae and Ribosome
18:00
Peptidoglycan: Gram + and Gram -
18:50
Bacterial Genomes and Reproduction
21:14
Bacterial Genomes
21:21
Reproduction of Bacteria
22:13
Transformation
23:26
Vector
24:34
Competent
25:15
Conjugation
25:53
Conjugation: F+ and R Plasmids
25:55
Example 1: Species
29:41
Example 2: Bacteria and Exchange of Genetic Material
32:31
Example 3: Ways in Which Bacteria are Beneficial to Other Organisms
33:48
Example 4: Domain Bacteria vs. Domain Archaea
34:53
Protists

1h 18m 48s

Intro
0:00
Classification of Protists
0:08
Classification of Protists
0:09
'Plant-like' Protists
2:06
'Animal-like' Protists
3:19
'Fungus-like' Protists
3:57
Serial Endosymbiosis Theory
5:15
Endosymbiosis Theory
5:33
Photosynthetic Protists
7:33
Life Cycles with a Diploid Adult
13:35
Life Cycles with a Diploid Adult
13:56
Life Cycles with a Haploid Adult
15:31
Life Cycles with a Haploid Adult
15:32
Alternation of Generations
17:22
Alternation of Generations: Multicellular Haploid & Diploid Phase
17:23
Plant-Like Protists
19:58
Euglenids
20:43
Dino Flagellates
22:57
Diatoms
26:07
Plant-Like Protists
28:44
Golden Algae
28:45
Brown Algeas
30:05
Plant-Like Protists
33:38
Red Algae
33:39
Green Algae
35:36
Green Algae: Chlamydomonus
37:44
Animal-Like Protists
40:04
Animal-Like Protists Overview
40:05
Sporozoans (Apicomplexans)
40:32
Alveolates
41:41
Sporozoans (Apicomplexans): Plasmodium & Malaria
42:59
Animal-Like Protists
48:44
Kinetoplastids
48:50
Example of Kinetoplastids: Trypanosomes & African Sleeping Sickness
49:30
Ciliate
50:42
Conjugation
53:16
Conjugation
53:26
Animal-Like Protists
57:08
Parabasilids
57:31
Diplomonads
59:06
Rhizopods
1:00:13
Forams
1:02:25
Radiolarians
1:03:28
Fungus-Like Protists
1:04:25
Fungus-Like Protists Overview
1:04:26
Slime Molds
1:05:15
Cellular Slime Molds: Feeding Stage
1:09:21
Oomycetes
1:11:15
Example 1: Alternation of Generations and Sexual Life Cycles
1:13:05
Example 2: Match Protists to Their Descriptions
1:14:12
Example 3: Three Structures that Protists Use for Motility
1:16:22
Example 4: Paramecium
1:17:04
Fungi

35m 24s

Intro
0:00
Introduction to Fungi
0:09
Introduction to Fungi
0:10
Mycologist
0:34
Examples of Fungi
0:45
Hyphae, Mycelia, Chitin, and Coencytic Fungi
2:26
Ancestral Protists
5:00
Role of Fungi in the Environment
5:35
Fungi as Decomposers
5:36
Mycorrrhiza
6:19
Lichen
8:52
Life Cycle of Fungi
11:32
Asexual Reproduction
11:33
Sexual Reproduction & Dikaryotic Cell
13:16
Chytridiomycota
18:12
Phylum Chytridiomycota
18:17
Zoospores
18:50
Zygomycota
19:07
Coenocytic & Zygomycota Life Cycle
19:08
Basidiomycota
24:27
Basidiomycota Overview
24:28
Basidiomycota Life Cycle
26:11
Ascomycota
28:00
Ascomycota Overview
28:01
Ascomycota Reproduction
28:50
Example 1: Fungi Fill in the Blank
31:02
Example 2: Name Two Roles Played by Fungi in the Environment
32:09
Example 3: Difference Between Diploid Cell and Dikaryon Cell
33:42
Example 4: Phylum of Fungi, Flagellated Spore, Coencytic
34:36
Invertebrates

1h 3m 3s

Intro
0:00
Porifera (Sponges)
0:33
Chordata
0:56
Porifera (Sponges): Sessile, Layers, Aceolomates, and Filter Feeders
1:24
Amoebocytes Cell
4:47
Choanocytes Cell
5:56
Sexual Reproduction
6:28
Cnidaria
8:05
Cnidaria Overview
8:06
Polyp & Medusa: Gastrovasular Cavity
8:29
Cnidocytes
9:42
Anthozoa
10:40
Cubozoa
11:23
Hydrozoa
11:53
Scyphoza
13:25
Platyhelminthes (Flatworms)
13:58
Flatworms: Tribloblastic, Bilateral Symmetry, and Cephalization
13:59
GI System
15:33
Excretory System
16:07
Nervous System
17:00
Turbellarians
17:36
Trematodes
18:42
Monageneans
21:32
Cestoda
21:55
Rotifera (Rotifers)
23:45
Rotifers: Digestive Tract, Pseudocoelem, and Stuctures
23:46
Reproduction: Parthenogenesis
25:33
Nematoda (Roundworms)
26:44
Nematoda (Roundworms)
26:45
Parasites: Pinworms & Hookworms
27:26
Annelida
28:36
Annelida Overview
28:37
Open Circulatory
29:21
Closed Circulatory
30:18
Nervous System
31:19
Excretory System
31:43
Oligochaete
32:07
Leeches
33:22
Polychaetes
34:42
Mollusca
35:26
Mollusca Features
35:27
Major Part 1: Visceral Mass
36:21
Major Part 2: Head-foot Region
36:49
Major Part 3: Mantle
37:13
Radula
37:49
Circulatory, Reproductive, Excretory, and Nervous System
38:14
Major Classes of Molluscs
39:12
Gastropoda
39:17
Polyplacophora
40:15
Bivales
40:41
Cephalopods
41:42
Arthropoda
43:35
Arthropoda Overview
43:36
Segmented Bodies
44:14
Exoskeleton
44:52
Jointed Appendages
45:28
Hemolyph, Excretory & Respiratory System
45:41
Myriapoda & Centipedes
47:15
Cheliceriforms
48:20
Crustcea
49:31
Herapoda
50:03
Echinodermata
52:59
Echinodermata
53:00
Watrer Vascular System
54:20
Selected Characteristics of Invertebrates
57:11
Selected Characteristics of Invertebrates
57:12
Example 1: Phylum Description
58:43
Example 2: Complex Animals
59:50
Example 3: Match Organisms to the Correct Phylum
1:01:03
Example 4: Phylum Arthropoda
1:02:01
Vertebrates

1h 7s

Intro
0:00
Phylum Chordata
0:06
Chordates Overview
0:07
Notochord and Dorsal Hollow Nerve Chord
1:24
Pharyngeal Clefts, Arches, and Post-anal Tail
3:41
Invertebrate Chordates
6:48
Lancelets
7:13
Tunicates
8:02
Hagfishes: Craniates
8:55
Vertebrate Chordates
10:41
Veterbrates Overview
10:42
Lampreys
11:00
Gnathostomes
12:20
Six Major Classes of Vertebrates
12:53
chondrichthyes
14:23
Chondrichthyes Overview
14:24
Ectothermic and Endothermic
14:42
Sharks: Lateral Line System, Neuromastsn, and Gills
15:27
Oviparous and Viviparous
17:23
Osteichthyes (Bony Fishes)
18:12
Osteichythes (Bony Fishes) Overview
18:13
Operculum
19:05
Swim Bladder
19:53
Ray-Finned Fishes
20:34
Lobe-Finned Fishes
20:58
Tetrapods
22:36
Tetrapods: Definition and Examples
22:37
Amphibians
23:53
Amphibians Overview
23:54
Order Urodela
25:51
Order Apoda
27:03
Order Anura
27:55
Reptiles
30:19
Reptiles Overview
30:20
Amniotes
30:37
Examples of Reptiles
32:46
Reptiles: Ectotherms, Gas Exchange, and Heart
33:40
Orders of Reptiles
34:17
Sphenodontia, Squamata, Testudines, and Crocodilia
34:21
Birds
36:09
Birds and Dinosaurs
36:18
Theropods
38:00
Birds: High Metabolism, Respiratory System, Lungs, and Heart
39:04
Birds: Endothermic, Bones, and Feathers
40:15
Mammals
42:33
Mammals Overview
42:35
Diaphragm and Heart
42:57
Diphydont
43:44
Synapsids
44:41
Monotremes
46:36
Monotremes
46:37
Marsupials
47:12
Marsupials: Definition and Examples
47:16
Convergent Evolution
48:09
Eutherians (Placental Mammals)
49:42
Placenta
49:43
Order Carnivora
50:48
Order Raodentia
51:00
Order Cetaceans
51:14
Primates
51:41
Primates Overview
51:42
Nails and Hands
51:58
Vision
52:51
Social Care for Young
53:28
Brain
53:43
Example 1: Distinguishing Characteristics of Chordates
54:33
Example 2: Match Description to Correct Term
55:56
Example 3: Bird's Anatomy
57:38
Example 4: Vertebrate Animal, Marine Environment, and Ectothermic
59:14
Section 9: Plants
Seedless Plants

34m 31s

Intro
0:00
Origin and Classification of Plants
0:06
Origin and Classification of Plants
0:07
Non-Vascular vs. Vascular Plants
1:29
Seedless Vascular & Seed Plants
2:28
Angiosperms & Gymnosperms
2:50
Alternation of Generations
3:54
Alternation of Generations
3:55
Bryophytes
7:58
Overview of Bryrophytes
7:59
Example: Moss Gametophyte
9:29
Example: Moss Sporophyte
9:50
Moss Life Cycle
10:12
Moss Life Cycle
10:13
Seedless Vascular Plants
13:23
Vascular Structures: Cell Walls, and Lignin
13:24
Homosporous
17:11
Heterosporous
17:48
Adaptations to Life on land
21:10
Adaptation 1: Cell Walls
21:38
Adaptation 2: Vascular Plants
21:59
Adaptation 3 : Xylem & Phloem
22:31
Adaptation 4: Seeds
23:07
Adaptation 5: Pollen
23:35
Adaptation 6: Stomata
24:45
Adaptation 7: Reduced Gametophyte Generation
25:32
Example 1: Bryophytes
26:39
Example 2: Sporangium, Lignin, Gametophyte, and Antheridium
28:34
Example 3: Adaptations to Life on Land
29:47
Example 4: Life Cycle of Plant
32:06
Plant Structure

1h 1m 21s

Intro
0:00
Plant Tissue
0:05
Dermal Tissue
0:15
Vascular Tissue
0:39
Ground Tissue
1:31
Cell Types in Plants
2:14
Parenchyma Cells
2:24
Collenchyma Cells
3:21
Sclerenchyma Cells
3:59
Xylem
5:04
Xylem: Tracheids and Vessel Elements
6:12
Gymnosperms vs. Angiosperms
7:53
Phloem
8:37
Phloem: Structures and Function
8:38
Sieve-Tube Elements
8:45
Companion Cells & Sieve Plates
9:11
Roots
10:08
Taproots & Fibrous
10:09
Aerial Roots & Prop Roots
11:41
Structures and Functions of Root: Dicot & Monocot
13:00
Pericyle
16:57
The Nitrogen Cylce
18:05
The Nitrogen Cycle
18:06
Mycorrhizae
24:20
Mycorrhizae
24:23
Ectomycorrhiza
26:03
Endomycorrhiza
26:25
Stems
26:53
Stems
26:54
Vascular Bundles of Monocots and Dicots
28:18
Leaves
29:48
Blade & Petiole
30:13
Upper Epidermis, Lower Epidermis & Cuticle
30:39
Ground Tissue, Palisade Mesophyll, Spongy Mesophyll
31:35
Stomata Pores
33:23
Guard Cells
34:15
Vascular Tissues: Vascular Bundles and Bundle Sheath
34:46
Stomata
36:12
Stomata & Gas Exchange
36:16
Guard Cells, Flaccid, and Turgid
36:43
Water Potential
38:03
Factors for Opening Stoma
40:35
Factors Causing Stoma to Close
42:44
Overview of Plant Growth
44:23
Overview of Plant Growth
44:24
Primary Plant Growth
46:19
Apical Meristems
46:25
Root Growth: Zone of Cell Division
46:44
Root Growth: Zone of Cell Elongation
47:35
Root Growth: Zone of Cell Differentiation
47:55
Stem Growth: Leaf Primodia
48:16
Secondary Plant Growth
48:48
Secondary Plant Growth Overview
48:59
Vascular Cambium: Secondary Xylem and Phloem
49:38
Cork Cambium: Periderm and Lenticels
51:10
Example 1: Leaf Structures
53:30
Example 2: List Three Types of Plant Tissue and their Major Functions
55:13
Example 3: What are Two Factors that Stimulate the Opening or Closing of Stomata?
56:58
Example 4: Plant Growth
59:18
Gymnosperms and Angiosperms

1h 1m 51s

Intro
0:00
Seed Plants
0:22
Sporopollenin
0:58
Heterosporous: Megasporangia
2:49
Heterosporous: Microsporangia
3:19
Gymnosperms
5:20
Gymnosperms
5:21
Gymnosperm Life Cycle
7:30
Gymnosperm Life Cycle
7:31
Flower Structure
15:15
Petal & Pollination
15:48
Sepal
16:52
Stamen: Anther, Filament
17:05
Pistill: Stigma, Style, Ovule, Ovary
17:55
Complete Flowers
20:14
Angiosperm Gametophyte Formation
20:47
Male Gametophyte: Microsporocytes, Microsporangia & Meiosis
20:57
Female Gametophyte: Megasporocytes & Meiosis
24:22
Double Fertilization
25:43
Double Fertilization: Pollen Tube and Endosperm
25:44
Angiosperm Life Cycle
29:43
Angiosperm Life Cycle
29:48
Seed Structure and Development
33:37
Seed Structure and Development
33:38
Pollen Dispersal
37:53
Abiotic
38:28
Biotic
39:30
Prevention of Self-Pollination
40:48
Mechanism 1
41:08
Mechanism 2: Dioecious
41:37
Mechanism 3
42:32
Self-Incompatibility
43:08
Gametophytic Self-Incompatibility
44:38
Sporophytic Self-Incompatibility
46:50
Asexual Reproduction
48:33
Asexual Reproduction & Vegetative Propagation
48:34
Graftiry
50:19
Monocots and Dicots
51:34
Monocots vs.Dicots
51:35
Example 1: Double Fertilization
54:43
Example 2: Mechanisms of Self-Fertilization
56:02
Example 3: Monocots vs. Dicots
58:11
Example 4: Flower Structures
1:00:11
Transport of Nutrients and Water in Plants

40m 30s

Intro
0:00
Review of Plant Cell Structure
0:14
Cell Wall, Plasma Membrane, Middle lamella, and Cytoplasm
0:15
Plasmodesmata, Chloroplasts, and Central Vacuole
3:24
Water Absorption by Plants
4:28
Root Hairs and Mycorrhizae
4:30
Osmosis and Water Potential
5:41
Apoplast and Symplast Pathways
10:01
Apoplast and Symplast Pathways
10:02
Xylem Structure
21:02
Tracheids and Vessel Elements
21:03
Bulk Flow
23:00
Transpiration
23:26
Cohesion
25:10
Adhesion
26:10
Phloem Structure
27:25
Pholem
27:26
Sieve-Tube Elements
27:48
Companion Cells
28:17
Translocation
28:42
Sugar Source and Sugar Sink Overview
28:43
Example of Sugar Sink
30:01
Example of Sugar Source
30:48
Example 1: Match the Following Terms to their Description
33:17
Example 2: Water Potential
34:58
Example 3: Bulk Flow
36:56
Example 4: Sugar Sink and Sugar Source
38:33
Plant Hormones and Tropisms

48m 10s

Intro
0:00
Plant Cell Signaling
0:17
Plant Cell Signaling Overview
0:18
Step 1: Reception
1:03
Step 2: Transduction
2:32
Step 3: Response
2:58
Second Messengers
3:52
Protein Kinases
4:42
Auxins
6:14
Auxins
6:18
Indoleacetic Acid (IAA)
7:23
Cytokinins and Gibberellins
11:10
Cytokinins: Apical Dominance & Delay of Aging
11:16
Gibberellins: 'Bolting'
13:51
Ethylene
15:33
Ethylene
15:34
Positive Feedback
15:46
Leaf Abscission
18:05
Mechanical Stress: Triple Response
19:36
Abscisic Acid
21:10
Abscisic Acid
21:15
Tropisms
23:11
Positive Tropism
23:50
Negative Tropism
24:07
Statoliths
26:21
Phytochromes and Photoperiodism
27:48
Phytochromes: PR and PFR
27:56
Circadian Rhythms
32:06
Photoperiod
33:13
Photoperiodism
33:38
Gerner & Allard
34:35
Short-Day Plant
35:22
Long-Day Plant
37:00
Example 1: Plant Hormones
41:28
Example 2: Cytokinins & Gibberellins
43:00
Example 3: Match the Following Terms to their Description
44:46
Example 4: Hormones & Cell Response
46:14
Section 10: Animal Structure and Physiology
The Respiratory System

48m 14s

Intro
0:00
Gas Exchange in Animals
0:17
Respiration
0:19
Ventilation
1:09
Characteristics of Respiratory Surfaces
1:53
Gas Exchange in Aquatic Animals
3:05
Simple Aquatic Animals
3:06
Gills & Gas Exchange in Complex Aquatic Animals
3:49
Countercurrent Exchange
6:12
Gas Exchange in Terrestrial Animals
13:46
Earthworms
14:07
Internal Respiratory
15:35
Insects
16:55
Circulatory Fluid
19:06
The Human Respiratory System
21:21
Nasal Cavity, Pharynx, Larynx, and Epiglottis
21:50
Bronchus, Bronchiole, Trachea, and Alveoli
23:38
Pulmonary Surfactants
28:05
Circulatory System: Hemoglobin
29:13
Ventilation
30:28
Inspiration/Expiration: Diaphragm, Thorax, and Abdomen
30:33
Breathing Control Center: Regulation of pH
34:34
Example 1: Tracheal System in Insects
39:08
Example 2: Countercurrent Exchange
42:09
Example 3: Respiratory System
44:10
Example 4: Diaphragm, Ventilation, pH, and Regulation of Breathing
45:31
The Circulatory System

1h 20m 21s

Intro
0:00
Types of Circulatory Systems
0:07
Circulatory System Overview
0:08
Open Circulatory System
3:19
Closed Circulatory System
5:58
Blood Vessels
7:51
Arteries
8:16
Veins
10:01
Capillaries
12:35
Vasoconstriction and Vasodilation
13:10
Vasoconstriction
13:11
Vasodilation
13:47
Thermoregulation
14:32
Blood
15:53
Plasma
15:54
Cellular Component: Red Blood Cells
17:41
Cellular Component: White Blood Cells
20:18
Platelets
21:14
Blood Types
21:35
Clotting
27:04
Blood, Fibrin, and Clotting
27:05
Hemophilia
30:26
The Heart
31:09
Structures and Functions of the Heart
31:19
Pulmonary and Systemic Circulation
40:20
Double Circuit: Pulmonary Circuit and Systemic Circuit
40:21
The Cardiac Cycle
42:35
The Cardiac Cycle
42:36
Autonomic Nervous System
50:00
Hemoglobin
51:25
Hemoglobin & Hemocyanin
51:26
Oxygen-Hemoglobin Dissociation Curve
55:30
Oxygen-Hemoglobin Dissociation Curve
55:44
Transport of Carbon Dioxide
1:06:31
Transport of Carbon Dioxide
1:06:37
Example 1: Pathway of Blood
1:12:48
Example 2: Oxygenated Blood, Pacemaker, and Clotting
1:15:24
Example 3: Vasodilation and Vasoconstriction
1:16:19
Example 4: Oxygen-Hemoglobin Dissociation Curve
1:18:13
The Digestive System

56m 11s

Intro
0:00
Introduction to Digestion
0:07
Digestive Process
0:08
Intracellular Digestion
0:45
Extracellular Digestion
1:44
Types of Digestive Tracts
2:08
Gastrovascular Cavity
2:09
Complete Gastrointestinal Tract (Alimentary Canal)
3:54
'Crop'
4:43
The Human Digestive System
5:41
Structures of the Human Digestive System
5:47
The Oral Cavity and Esophagus
7:47
Mechanical & Chemical Digestion
7:48
Salivary Glands
8:55
Pharynx and Epigloltis
9:43
Peristalsis
11:35
The Stomach
12:57
Lower Esophageal Sphincter
13:00
Gastric Gland, Parietal Cells, and Pepsin
14:32
Mucus Cell
15:48
Chyme & Pyloric Sphincter
17:32
The Pancreas
18:31
Endocrine and Exocrine
19:03
Amylase
20:05
Proteases
20:51
Lipases
22:20
The Liver
23:08
The Liver & Production of Bile
23:09
The Small Intestine
24:37
The Small Intestine
24:38
Duodenum
27:44
Intestinal Enzymes
28:41
Digestive Enzyme
33:30
Site of Production: Mouth
33:43
Site of Production: Stomach
34:03
Site of Production: Pancreas
34:16
Site of Production: Small Intestine
36:18
Absorption of Nutrients
37:51
Absorption of Nutrients: Jejunum and Ileum
37:52
The Large Intestine
44:52
The Large Intestine: Colon, Cecum, and Rectum
44:53
Regulation of Digestion by Hormones
46:55
Gastrin
47:21
Secretin
47:50
Cholecystokinin (CCK)
48:00
Example 1: Intestinal Cell, Bile, and Digestion of Fats
48:29
Example 2: Matching
51:06
Example 3: Digestion and Absorption of Starch
52:18
Example 4: Large Intestine and Gastric Fluids
54:52
The Excretory System

1h 12m 14s

Intro
0:00
Nitrogenous Wastes
0:08
Nitrogenous Wastes Overview
0:09
NH3
0:39
Urea
2:43
Uric Acid
3:31
Osmoregulation
4:56
Osmoregulation
5:05
Saltwater Fish vs. Freshwater Fish
8:58
Types of Excretory Systems
13:42
Protonephridia
13:50
Metanephridia
16:15
Malpighian Tubule
19:05
The Human Excretory System
20:45
Kidney, Ureter, bladder, Urethra, Medula, and Cortex
20:53
Filtration, Reabsorption and Secretion
22:53
Filtration
22:54
Reabsorption
24:16
Secretion
25:20
The Nephron
26:23
The Nephron
26:24
The Nephron, cont.
41:45
Descending Loop of Henle
41:46
Ascending Loop of Henle
45:45
Antidiuretic Hormone
54:30
Antidiuretic Hormone (ADH)
54:31
Aldosterone
58:58
Aldosterone
58:59
Example 1: Nephron of an Aquatic Mammal
1:04:21
Example 2: Uric Acid & Saltwater Fish
1:06:36
Example 3: Nephron
1:09:14
Example 4: Gastrointestinal Infection
1:10:41
The Endocrine System

51m 12s

Intro
0:00
The Endocrine System Overview
0:07
Thyroid
0:08
Exocrine
1:56
Pancreas
2:44
Paracrine Signaling
4:06
Pheromones
5:15
Mechanisms of Hormone Action
6:06
Reception, Transduction, and Response
7:06
Classes of Hormone
10:05
Negative Feedback: Testosterone Example
12:16
The Pancreas
15:11
The Pancreas & islets of Langerhan
15:12
Insulin
16:02
Glucagon
17:28
The Anterior Pituitary
19:25
Thyroid Stimulating Hormone
20:24
Adrenocorticotropic Hormone
21:16
Follide Stimulating Hormone
22:04
Luteinizing Hormone
22:45
Growth Hormone
23:45
Prolactin
24:24
Melanocyte Stimulating Hormone
24:55
The Hypothalamus and Posterior Pituitary
25:45
Hypothalamus, Oxytocin, Antidiuretic Hormone (ADH), and Posterior Pituitary
25:46
The Adrenal Glands
31:20
Adrenal Cortex
31:56
Adrenal Medulla
34:29
The Thyroid
35:54
Thyroxine
36:09
Calcitonin
40:27
The Parathyroids
41:44
Parathyroids Hormone (PTH)
41:45
The Ovaries and Testes
43:32
Estrogen, Progesterone, and Testosterone
43:33
Example 1: Match the Following Hormones with their Descriptions
45:38
Example 2: Pancreas, Endocrine Organ & Exocrine Organ
47:06
Example 3: Insulin and Glucagon
48:28
Example 4: Increased Level of Cortisol in Blood
50:25
The Nervous System

1h 10m 38s

Intro
0:00
Types of Nervous Systems
0:28
Nerve Net
0:37
Flatworm
1:07
Cephalization
1:52
Arthropods
2:44
Echinoderms
3:11
Nervous System Organization
3:40
Nervous System Organization Overview
3:41
Automatic Nervous System: Sympathetic & Parasympathetic
4:42
Neuron Structure
6:57
Cell Body & Dendrites
7:16
Axon & Axon Hillock
8:20
Synaptic Terminals, Mylenin, and Nodes of Ranvier
9:01
Pre-synaptic and Post-synaptic Cells
10:16
Pre-synaptic Cells
10:17
Post-synaptic Cells
11:05
Types of Neurons
11:50
Sensory Neurons
11:54
Motor Neurons
13:12
Interneurons
14:24
Resting Potential
15:14
Membrane Potential
15:25
Resting Potential: Chemical Gradient
16:06
Resting Potential: Electrical Gradient
19:18
Gated Ion Channels
24:40
Voltage-Gated & Ligand-Gated Ion Channels
24:48
Action Potential
30:09
Action Potential Overview
30:10
Step 1
32:07
Step 2
32:17
Step 3
33:12
Step 4
35:14
Step 5
36:39
Action Potential Transmission
39:04
Action Potential Transmission
39:05
Speed of Conduction
41:19
Saltatory Conduction
42:58
The Synapse
44:17
The Synapse: Presynaptic & Postsynaptic Cell
44:31
Examples of Neurotransmitters
50:05
Brain Structure
51:57
Meniges
52:19
Cerebrum
52:56
Corpus Callosum
53:13
Gray & White Matter
53:38
Cerebral Lobes
55:35
Cerebellum
56:00
Brainstem
56:30
Medulla
56:51
Pons
57:22
Midbrain
57:55
Thalamus
58:25
Hypothalamus
58:58
Ventricles
59:51
The Spinal Cord
1:00:29
Sensory Stimuli
1:00:30
Reflex Arc
1:01:41
Example 1: Automatic Nervous System
1:04:38
Example 2: Synaptic Terminal and the Release of Neurotransmitters
1:06:22
Example 3: Volted-Gated Ion Channels
1:08:00
Example 4: Neuron Structure
1:09:26
Musculoskeletal System

39m 29s

Intro
0:00
Skeletal System Types and Function
0:30
Skeletal System
0:31
Exoskeleton
1:34
Endoskeleton
2:32
Skeletal System Components
2:55
Bone
3:06
Cartilage
5:04
Tendons
6:18
Ligaments
6:34
Skeletal Muscle
6:52
Skeletal Muscle
7:24
Sarcomere
9:50
The Sliding Filament Theory
13:12
The Sliding Filament Theory: Muscle Contraction
13:13
The Neuromuscular Junction
17:24
The Neuromuscular Junction: Motor Neuron & Muscle Fiber
17:26
Sarcolemma, Sarcoplasmic
21:54
Tropomyosin & Troponin
23:35
Summation and Tetanus
25:26
Single Twitch, Summation of Two Twitches, and Tetanus
25:27
Smooth Muscle
28:50
Smooth Muscle
28:58
Cardiac Muscle
30:40
Cardiac Muscle
30:42
Summary of Muscle Types
32:07
Summary of Muscle Types
32:08
Example 1: Contraction and Skeletal Muscle
33:15
Example 2: Skeletal Muscle and Smooth Muscle
36:23
Example 3: Muscle Contraction, Bone, and Nonvascularized Connective Tissue
37:31
Example 4: Sarcomere
38:17
The Immune System

1h 24m 28s

Intro
0:00
The Lymphatic System
0:16
The Lymphatic System Overview
0:17
Function 1
1:23
Function 2
2:27
Barrier Defenses
3:41
Nonspecific vs. Specific Immune Defenses
3:42
Barrier Defenses
5:12
Nonspecific Cellular Defenses
7:50
Nonspecific Cellular Defenses Overview
7:53
Phagocytes
9:29
Neutrophils
11:43
Macrophages
12:15
Natural Killer Cells
12:55
Inflammatory Response
14:19
Complement
18:16
Interferons
18:40
Specific Defenses - Acquired Immunity
20:12
T lymphocytes and B lymphocytes
20:13
B Cells
23:35
B Cells & Humoral Immunity
23:41
Clonal Selection
29:50
Clonal Selection
29:51
Primary Immune Response
34:28
Secondary Immune Response
35:31
Cytotoxic T Cells
38:41
Helper T Cells
39:20
Major Histocompatibility Complex Molecules
40:44
Major Histocompatibility Complex Molecules
40:55
Helper T Cells
52:36
Helper T Cells
52:37
Mechanisms of Antibody Action
59:00
Mechanisms of Antibody Action
59:01
Opsonization
1:00:01
Complement System
1:01:57
Classes of Antibodies
1:02:45
IgM
1:03:01
IgA
1:03:17
IgG
1:03:53
IgE
1:04:10
Passive and Active Immunity
1:05:00
Passive Immunity
1:05:01
Active Immunity
1:07:49
Recognition of Self and Non-Self
1:09:32
Recognition of Self and Non-Self
1:09:33
Self-Tolerance & Autoimmune Diseases
1:10:50
Immunodeficiency
1:13:27
Immunodeficiency
1:13:28
Chemotherapy
1:13:56
AID
1:14:27
Example 1: Match the Following Terms with their Descriptions
1:15:26
Example 2: Three Components of Non-specific Immunity
1:17:59
Example 3: Immunodeficient
1:21:19
Example 4: Self-tolerance and Autoimmune Diseases
1:23:07
Section 11: Animal Reproduction and Development
Reproduction

1h 1m 41s

Intro
0:00
Asexual Reproduction
0:17
Fragmentation
0:53
Fission
1:54
Parthenogenesis
2:38
Sexual Reproduction
4:00
Sexual Reproduction
4:01
Hermaphrodite
8:08
The Male Reproduction System
8:54
Seminiferous Tubules & Leydig Cells
8:55
Epididymis
9:48
Seminal Vesicle
11:19
Bulbourethral
12:37
The Female Reproductive System
13:25
Ovaries
13:28
Fallopian
14:50
Endometrium, Uterus, Cilia, and Cervix
15:03
Mammary Glands
16:44
Spermatogenesis
17:08
Spermatogenesis
17:09
Oogenesis
21:01
Oogenesis
21:02
The Menstrual Cycle
27:56
The Menstrual Cycle: Ovarian and Uterine Cycle
27:57
Summary of the Ovarian and Uterine Cycles
42:54
Ovarian
42:55
Uterine
44:51
Oxytocin and Prolactin
46:33
Oxytocin
46:34
Prolactin
47:00
Regulation of the Male Reproductive System
47:28
Hormones: GnRH, LH, FSH, and Testosterone
47:29
Fertilization
50:11
Fertilization
50:12
Structures of Egg
50:28
Acrosomal Reaction
51:36
Cortical Reaction
53:09
Example 1: List Three Differences between Spermatogenesis and oogenesis
55:36
Example 2: Match the Following Terms to their Descriptions
57:34
Example 3: Pregnancy and the Ovarian Cycle
58:44
Example 4: Hormone
1:00:43
Development

50m 5s

Intro
0:00
Cleavage
0:31
Cleavage
0:32
Meroblastic
2:06
Holoblastic Cleavage
3:23
Protostomes
4:34
Deuterostomes
5:13
Totipotent
5:52
Blastula Formation
6:42
Blastula
6:46
Gastrula Formation
8:12
Deuterostomes
11:02
Protostome
11:44
Ectoderm
12:17
Mesoderm
12:55
Endoderm
13:40
Cytoplasmic Determinants
15:19
Cytoplasmic Determinants
15:23
The Bird Embryo
22:52
Cleavage
23:35
Blastoderm
23:55
Primitive Streak
25:38
Migration and Differentiation
27:09
Extraembryonic Membranes
28:33
Extraembryonic Membranes
28:34
Chorion
30:02
Yolk Sac
30:36
Allantois
31:04
The Mammalian Embryo
32:18
Cleavage
32:28
Blastocyst
32:44
Trophoblast
34:37
Following Implantation
35:48
Organogenesis
37:04
Organogenesis, Notochord and Neural Tube
37:05
Induction
40:15
Induction
40:39
Fate Mapping
41:40
Example 1: Processes and Stages of Embryological Development
42:49
Example 2: Transplanted Cells
44:33
Example 3: Germ Layer
46:41
Example 4: Extraembryonic Membranes
47:28
Section 12: Animal Behavior
Animal Behavior

47m 48s

Intro
0:00
Introduction to Animal Behavior
0:05
Introduction to Animal Behavior
0:06
Ethology
1:04
Proximate Cause & Ultimate Cause
1:46
Fixed Action Pattern
3:07
Sign Stimulus
3:40
Releases and Example
3:55
Exploitation and Example
7:23
Learning
8:56
Habituation, Associative Learning, and Imprinting
8:57
Habituation
10:03
Habituation: Definition and Example
10:04
Associative Learning
11:47
Classical
12:19
Operant Conditioning
13:40
Positive & Negative Reinforcement
14:59
Positive & Negative Punishment
16:13
Extinction
17:28
Imprinting
17:47
Imprinting: Definition and Example
17:48
Social Behavior
20:12
Cooperation
20:38
Agonistic
21:37
Dorminance Heirarchies
23:23
Territoriality
24:08
Altruism
24:55
Communication
26:56
Communication
26:57
Mating
32:38
Mating Overview
32:40
Promiscuous
33:13
Monogamous
33:32
Polygamous
33:48
Intrasexual
34:22
Intersexual Selection
35:08
Foraging
36:08
Optimal Foraging Model
36:39
Foraging
37:47
Movement
39:12
Kinesis
39:20
Taxis
40:17
Migration
40:54
Lunar Cycles
42:02
Lunar Cycles
42:08
Example 1: Types of Conditioning
43:19
Example 2: Match the Following Terms to their Descriptions
44:12
Example 3: How is the Optimal Foraging Model Used to Explain Foraging Behavior
45:47
Example 4: Learning
46:54
Section 13: Ecology
Biomes

58m 49s

Intro
0:00
Ecology
0:08
Ecology
0:14
Environment
0:22
Integrates
1:41
Environment Impacts
2:20
Population and Distribution
3:20
Population
3:21
Range
4:50
Potential Range
5:10
Abiotic
5:46
Biotic
6:22
Climate
7:55
Temperature
8:40
Precipitation
10:00
Wind
10:37
Sunlight
10:54
Macroclimates & Microclimates
11:31
Other Abiotic Factors
12:20
Geography
12:28
Water
13:17
Soil and Rocks
13:48
Sunlight
14:42
Sunlight
14:43
Seasons
15:43
June Solstice, December Solstice, March Equinox, and September Equinox
15:44
Tropics
19:00
Seasonability
19:39
Wind and Weather Patterns
20:44
Vertical Circulation
20:51
Surface Wind Patterns
25:18
Local Climate Effects
26:51
Local Climate Effects
26:52
Terrestrial Biomes
30:04
Biome
30:05
Forest
31:02
Tropical Forest
32:00
Tropical Forest
32:01
Temperate Broadleaf Forest
32:55
Temperate Broadleaf Forest
32:56
Coniferous/Taiga Forest
34:10
Coniferous/Taiga Forest
34:11
Desert
36:05
Desert
36:06
Grassland
37:45
Grassland
37:46
Tundra
40:09
Tundra
40:10
Freshwater Biomes
42:25
Freshwater Biomes: Zones
42:27
Eutrophic Lakes
44:24
Oligotrophic Lakes
45:01
Lakes Turnover
46:03
Rivers
46:51
Wetlands
47:40
Estuary
48:11
Marine Biomes
48:45
Marine Biomes: Zones
48:46
Example 1: Diversity of Life
52:18
Example 2: Marine Biome
53:08
Example 3: Season
54:20
Example 4: Biotic vs. Abiotic
55:54
Population

41m 16s

Intro
0:00
Population
0:07
Size 'N'
0:16
Density
0:41
Dispersion
1:01
Measure Population: Count Individuals, Sampling, and Proxymeasure
2:26
Mortality
7:29
Mortality and Survivorship
7:30
Age Structure Diagrams
11:52
Expanding with Rapid Growth, Expanding, and Stable
11:58
Population Growth
15:39
Biotic Potential & Exponential Growth
15:43
Logistic Population Growth
19:07
Carrying Capacity (K)
19:18
Limiting Factors
20:55
Logistic Model and Oscillation
22:55
Logistic Model and Oscillation
22:56
Changes to the Carrying Capacity
24:36
Changes to the Carrying Capacity
24:37
Growth Strategies
26:07
'r-selected' or 'r-strategist'
26:23
'K-selected' or 'K-strategist'
27:47
Human Population
30:15
Human Population and Exponential Growth
30:21
Case Study - Lynx and Hare
31:54
Case Study - Lynx and Hare
31:55
Example 1: Estimating Population Size
34:35
Example 2: Population Growth
36:45
Example 3: Carrying Capacity
38:17
Example 4: Types of Dispersion
40:15
Communities

1h 6m 26s

Intro
0:00
Community
0:07
Ecosystem
0:40
Interspecific Interactions
1:14
Competition
2:45
Competition Overview
2:46
Competitive Exclusion
3:57
Resource Partitioning
4:45
Character Displacement
6:22
Predation
7:46
Predation
7:47
True Predation
8:05
Grazing/ Herbivory
8:39
Predator Adaptation
10:13
Predator Strategies
10:22
Physical Features
11:02
Prey Adaptation
12:14
Prey Adaptation
12:23
Aposematic Coloration
13:35
Batesian Mimicry
14:32
Size
15:42
Parasitism
16:48
Symbiotic Relationship
16:54
Ectoparasites
18:31
Endoparasites
18:53
Hyperparisitism
19:21
Vector
20:08
Parasitoids
20:54
Mutualism
21:23
Resource - Resource mutualism
21:34
Service - Resource Mutualism
23:31
Service - Service Mutualism: Obligate & Facultative
24:23
Commensalism
26:01
Commensalism
26:03
Symbiosis
27:31
Trophic Structure
28:35
Producers & Consumers: Autotrophs & Heterotrophs
28:36
Food Chain
33:26
Producer & Consumers
33:38
Food Web
39:01
Food Web
39:06
Significant Species within Communities
41:42
Dominant Species
41:50
Keystone Species
42:44
Foundation Species
43:41
Community Dynamics and Disturbances
44:31
Disturbances
44:33
Duration
47:01
Areal Coverage
47:22
Frequency
47:48
Intensity
48:04
Intermediate Level of Disturbance
48:20
Ecological Succession
50:29
Primary and Secondary Ecological Succession
50:30
Example 1: Competition Situation & Outcome
57:18
Example 2: Food Chains
1:00:08
Example 3: Ecological Units
1:02:44
Example 4: Disturbances & Returning to the Original Climax Community
1:04:30
Energy and Ecosystems

57m 42s

Intro
0:00
Ecosystem: Biotic & Abiotic Components
0:15
First Law of Thermodynamics & Energy Flow
0:40
Gross Primary Productivity (GPP)
3:52
Net Primary Productivity (NPP)
4:50
Biogeochemical Cycles
7:16
Law of Conservation of Mass & Biogeochemical Cycles
7:17
Water Cycle
10:55
Water Cycle
10:57
Carbon Cycle
17:52
Carbon Cycle
17:53
Nitrogen Cycle
22:40
Nitrogen Cycle
22:41
Phosphorous Cycle
29:34
Phosphorous Cycle
29:35
Climate Change
33:20
Climate Change
33:21
Eutrophication
39:38
Nitrogen
40:34
Phosphorous
41:29
Eutrophication
42:55
Example 1: Energy and Ecosystems
45:28
Example 2: Atmospheric CO2
48:44
Example 3: Nitrogen Cycle
51:22
Example 4: Conversion of a Forest near a Lake to Farmland
53:20
Section 14: Laboratory Review
Laboratory Review

2h 4m 30s

Intro
0:00
Lab 1: Diffusion and Osmosis
0:09
Lab 1: Diffusion and Osmosis
0:10
Lab 1: Water Potential
11:55
Lab 1: Water Potential
11:56
Lab 2: Enzyme Catalysis
18:30
Lab 2: Enzyme Catalysis
18:31
Lab 3: Mitosis and Meiosis
27:40
Lab 3: Mitosis and Meiosis
27:41
Lab 3: Mitosis and Meiosis
31:50
Ascomycota Life Cycle
31:51
Lab 4: Plant Pigments and Photosynthesis
40:36
Lab 4: Plant Pigments and Photosynthesis
40:37
Lab 5: Cell Respiration
49:56
Lab 5: Cell Respiration
49:57
Lab 6: Molecular Biology
55:06
Lab 6: Molecular Biology & Transformation 1st Part
55:07
Lab 6: Molecular Biology
1:01:16
Lab 6: Molecular Biology 2nd Part
1:01:17
Lab 7: Genetics of Organisms
1:07:32
Lab 7: Genetics of Organisms
1:07:33
Lab 7: Chi-square Analysis
1:13:00
Lab 7: Chi-square Analysis
1:13:03
Lab 8: Population Genetics and Evolution
1:20:41
Lab 8: Population Genetics and Evolution
1:20:42
Lab 9: Transpiration
1:24:02
Lab 9: Transpiration
1:24:03
Lab 10: Physiology of the Circulatory System
1:31:05
Lab 10: Physiology of the Circulatory System
1:31:06
Lab 10: Temperature and Metabolism in Ectotherms
1:38:25
Lab 10: Temperature and Metabolism in Ectotherms
1:38:30
Lab 11: Animal Behavior
1:40:52
Lab 11: Animal Behavior
1:40:53
Lab 12: Dissolved Oxygen & Aquatic Primary Productivity
1:45:36
Lab 12: Dissolved Oxygen & Aquatic Primary Productivity
1:45:37
Lab 12: Primary Productivity
1:49:06
Lab 12: Primary Productivity
1:49:07
Example 1: Chi-square Analysis
1:56:31
Example 2: Mitosis
1:59:28
Example 3: Transpiration of Plants
2:00:27
Example 4: Population Genetic
2:01:16
Section 15: The AP Biology Test
Understanding the Basics

13m 2s

Intro
0:00
AP Biology Structure
0:18
Section I
0:31
Section II
1:16
Scoring
2:04
The Four 'Big Ideas'
3:51
Process of Evolution
4:37
Biological Systems Utilize
4:44
Living Systems
4:55
Biological Systems Interact
5:03
Items to Bring to the Test
7:56
Test Taking Tips
9:53
Section 16: Practice Test (Barron's 4th Edition)
AP Biology Practice Exam: Section I, Part A, Multiple Choice Questions 1-31

1h 4m 29s

Intro
0:00
AP Biology Practice Exam
0:14
Multiple Choice 1
0:40
Multiple Choice 2
2:27
Multiple Choice 3
4:30
Multiple Choice 4
6:43
Multiple Choice 5
9:27
Multiple Choice 6
11:32
Multiple Choice 7
12:54
Multiple Choice 8
14:42
Multiple Choice 9
17:06
Multiple Choice 10
18:42
Multiple Choice 11
20:49
Multiple Choice 12
23:23
Multiple Choice 13
26:20
Multiple Choice 14
27:52
Multiple Choice 15
28:44
Multiple Choice 16
33:07
Multiple Choice 17
35:31
Multiple Choice 18
39:43
Multiple Choice 19
40:37
Multiple Choice 20
42:47
Multiple Choice 21
45:58
Multiple Choice 22
49:49
Multiple Choice 23
53:44
Multiple Choice 24
55:12
Multiple Choice 25
55:59
Multiple Choice 26
56:50
Multiple Choice 27
58:08
Multiple Choice 28
59:54
Multiple Choice 29
1:01:36
Multiple Choice 30
1:02:31
Multiple Choice 31
1:03:50
AP Biology Practice Exam: Section I, Part A, Multiple Choice Questions 32-63

50m 44s

Intro
0:00
AP Biology Practice Exam
0:14
Multiple Choice 32
0:27
Multiple Choice 33
4:14
Multiple Choice 34
5:12
Multiple Choice 35
6:51
Multiple Choice 36
10:46
Multiple Choice 37
11:27
Multiple Choice 38
12:17
Multiple Choice 39
13:49
Multiple Choice 40
17:02
Multiple Choice 41
18:27
Multiple Choice 42
19:35
Multiple Choice 43
21:10
Multiple Choice 44
23:35
Multiple Choice 45
25:00
Multiple Choice 46
26:20
Multiple Choice 47
28:40
Multiple Choice 48
30:14
Multiple Choice 49
31:24
Multiple Choice 50
32:45
Multiple Choice 51
33:41
Multiple Choice 52
34:40
Multiple Choice 53
36:12
Multiple Choice 54
38:06
Multiple Choice 55
38:37
Multiple Choice 56
40:00
Multiple Choice 57
41:18
Multiple Choice 58
43:12
Multiple Choice 59
44:25
Multiple Choice 60
45:02
Multiple Choice 61
46:10
Multiple Choice 62
47:54
Multiple Choice 63
49:01
AP Biology Practice Exam: Section I, Part B, Grid In

21m 52s

Intro
0:00
AP Biology Practice Exam
0:17
Grid In Question 1
0:29
Grid In Question 2
3:49
Grid In Question 3
11:04
Grid In Question 4
13:18
Grid In Question 5
17:01
Grid In Question 6
19:30
AP Biology Practice Exam: Section II, Long Free Response Questions

31m 22s

Intro
0:00
AP Biology Practice Exam
0:18
Free Response 1
0:29
Free Response 2
20:47
AP Biology Practice Exam: Section II, Short Free Response Questions

24m 41s

Intro
0:00
AP Biology Practice Exam
0:15
Free Response 3
0:26
Free Response 4
5:21
Free Response 5
8:25
Free Response 6
11:38
Free Response 7
14:48
Free Response 8
22:14
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Lecture Comments (21)

0 answers

Post by Anthony Villarama on September 25, 2018

She could have done better in explaining the Allosteric regulators.

1 answer

Last reply by: Dr Carleen Eaton
Fri Jan 29, 2016 10:58 AM

Post by Saakshi Dhingra on January 21, 2016

Hello Dr. Eaton. What is the difference between endergonic and exergonic reactions in comparison to endothermic and exothermic reactions?

1 answer

Last reply by: Dr Carleen Eaton
Tue Nov 18, 2014 4:39 PM

Post by Anmol Chowdhary on November 16, 2014

Hi Dr. Eaton,

How do enzyme activation and enzyme inhibition factors affect enzymatic speed?  The ones discussed were enzyme cofactors, temperature, pH, and substrate concentration.

Thank you

1 answer

Last reply by: Dr Carleen Eaton
Tue Mar 25, 2014 3:12 PM

Post by Emmanuel Nunes on March 14, 2014

Thank you  Dr Eaton for this great lecture

1 answer

Last reply by: Chrystal Wang
Sat Nov 9, 2019 10:01 PM

Post by manuel dihr on July 18, 2013

i think there might something wrong with the structure of ATP: there is no OH connecting ribose with triphosphate. otherwise oxygen would disobey the octett rule

1 answer

Last reply by: Dr Carleen Eaton
Tue Apr 9, 2013 1:58 PM

Post by Ikze Cho on April 9, 2013

all enzymes are proteins right?

1 answer

Last reply by: Dr Carleen Eaton
Wed May 9, 2012 3:58 PM

Post by Gayatri Arumugam on May 6, 2012

Would ATP be the product of an endergonic reaction?

1 answer

Last reply by: Dr Carleen Eaton
Mon Feb 27, 2012 11:07 PM

Post by Michael Mann on February 23, 2012

Hello,

In the video (5:01)when you are talking about delta G being negative and spontaneous and does not require energy input is that because there is always energy there?

M.Mann

1 answer

Last reply by: Dr Carleen Eaton
Wed Jan 18, 2012 12:09 PM

Post by Gaby Vazquez on January 16, 2012

Thank you Dr. Eaton! Excellent lecture, really clears concepts!

3 answers

Last reply by: Chrystal Wang
Sat Nov 9, 2019 10:15 PM

Post by felix michoutchenko on October 19, 2011

Isn't delta = 0 an equilibrium (neither spontaneous nor non-spontaneous)??

Enzymes

  • Δ G = ΔH – TΔS is the Gibbs free energy equation.
  • Reactions with a negative ΔG release energy; these are exergonic reactions.
  • Reactions with a positive ΔG absorb energy; these are endergonic reactions.
  • Enzymes increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They do not change the overall ΔG of a reaction.
  • Each enzyme binds only to specific substrates and catalyzes a particular reaction.
  • Enzyme activity is affected by substrate concentration, temperature, pH and the presence of cofactors. Enzyme activity may also be decreased through the effects of competitive or noncompetitive inhibitors.
  • Competitive inhibitors are similar in shape to the substrate. They bind to the enzyme’s active site and prevent the binding of the substrate.
  • Allosteric regulators affect an enzyme’s activity by binding to sites outside of the active site. Binding to these sites causes a conformational change in the active site.

Enzymes

Lecture Slides are screen-captured images of important points in the lecture. Students can download and print out these lecture slide images to do practice problems as well as take notes while watching the lecture.

  • Intro 0:00
  • Law of Thermodynamics 0:08
    • Thermodynamics
    • The First Law of Thermodynamics
    • The Second Law of Thermodynamics
    • Entropy
  • The Gibbs Free Energy Equation 3:07
    • The Gibbs Free Energy Equation
  • ATP 8:23
    • Adenosine Triphosphate (ATP)
    • Cellular Respiration
    • Catabolic Pathways
    • Anabolic Pathways
  • Enzymes 14:31
    • Enzymes
    • Enzymes and Exergonic Reaction
    • Enzymes and Endergonic Reaction
  • Enzyme Specificity 21:29
    • Substrate
    • Induced Fit
  • Factors Affecting Enzyme Activity 25:55
    • Substrate Concentration
    • pH
    • Temperature
    • Presence of Cofactors
  • Regulation of Enzyme Activity 31:12
    • Competitive Inhibitors
    • Noncompetitive Inhibitors
    • Feedback Inhibition
  • Allosteric Interactions 36:56
    • Allosteric Regulators
  • Example 1: Is the Inhibitor Competitive or Noncompetitive? 40:49
  • Example 2: Thermophiles 44:18
  • Example 3: Exergonic or Endergonic 46:09
  • Example 4: Energy Vs. Reaction Progress Graph 48:47

Transcription: Enzymes

Welcome to Educator.com.0000

Today is the first in a series of lessons on cellular energetics, and we are going to start out by focusing on enzymes.0002

To understand enzymes, you need to first understand energy.0010

We are going to start out with the discussion of some of the laws of thermodynamics.0015

Thermodynamics is the field that studies the conversion of energy between heat and other forms of energy. It is concerned with the transfer of energy.0020

And we are actually going to focus on two of the laws of thermodynamics and then, discuss enzymes.0031

The first law of thermodynamics states that energy cannot be created or destroyed. It can only be changed from one form to another.0037

The total amount of energy in matter in the universe remains constant.0048

It can change from one form to another, but it cannot be created or destroyed.0054

For example, you take in energy in a form of food, and the energy stored in the chemical bonds of the food can be released; and you could use that energy to take a walk for example.0060

You are using the energy from the food and transferring it into another form - kinetic energy - when you walk.0074

That is allowed. It is energy conversion.0081

The second law of thermodynamics states that the process of energy conversion, that I just discussed or energy transfer, increases the entropy of the universe.0084

What is entropy? Entropy is a measure of disorder.0096

Therefore, when energy is transferred or converted into another form, things become more disordered, more random, more chaotic.0108

The transfer of energy increases disorder in the universe.0117

When energy is transferred, it is not all conserved as usable energy. Some of the energy is converted to heat.0123

I mentioned that you could eat something. You could eat a sandwich, and then, you could use that energy to go walk converting it to kinetic energy.0132

However, not every single calorie that you eat is going to be converted into kinetic energy.0142

Not every little bit of that nutrient is going to go into making your legs move.0151

Some of it will be lost as heat. Heat is not usable energy.0155

Overall, the universe becomes more and more random because that heat, that unusable energy, contributes to the disorder of the universe overall.0161

Now, an individual situation could become more ordered.0171

You can go and clean up your room.0174

That is contributing to the order of your room, but taken as a whole, the universe is overall becoming more random; and the usable energy is decreasing.0176

In biology, we are often concerned with the portion of energy in a system that is available to do work, and this is known as the Gibbs free energy or just free energy.0188

This equation here is describing the change in free energy for a reaction, and this is called the Gibbs free energy equation.0198

Let's look at each part of this equation and discuss what it means.0206

Overall, it tells you the change in free energy at a constant temperature and pressure, so ΔG is the free energy change.0209

If we are talking about a chemical reaction, this would be the difference between the free energy of the products and the reactants.0219

The G of the final state, which would be the free energy of the products minus the free energy or G of the initial state of the reactants equals ΔH, so H is enthalpy.0229

ΔH gives you the change in enthalpy.0246

With biological reactions, this can just be thought of as the heat of the reaction for our purposes, so this is about the same as the heat of the reaction.0251

ΔS: I just described entropy, and S is entropy.0265

The change in entropy, increased entropy would mean an increase in disorder.0269

T is the temperature given in Kelvins.0279

The important thing to know is that if the ΔG is negative, the reaction is spontaneous.0289

If the ΔG is 0 or positive, the reaction is not spontaneous.0304

Now, what does that mean?0311

Spontaneous means that a reaction can take place without the input of energy. It does not require energy input.0313

This does not tell me anything about the speed of the reaction, the rate of the reaction.0327

It only tells me that the reaction can take place without the input of the energy,0331

whereas, a positive or 0 ΔG tells that for this reaction to occur, energy would have to be put into the system, so it requires the input of energy.0335

Alright, how could we end up with a -ΔG?0352

Looking at this equation, there are a couple of possibilities.0359

H could decrease. In other words, heat will be lost or increased TΔS, so what we could do here is increase in ΔS.0362

Overall, what would be happening is the system is increasing the disorder in the universe, so increased disorder.0380

If ΔH decreases or TΔS increases, either way, you are going to end up with a -ΔG, and the reaction will be a spontaneous.0392

If the reaction causes either a loss of heat going from reactants to products or an increase in disorder, either of those will result in a -ΔG and a spontaneous reaction.0401

The name for reactions that have a -ΔG in biology are known as exergonic reactions.0417

Exergonic reactions are spontaneous, and they have a -ΔG. Those with a positive or 0 ΔG are endergonic.0427

Frequently in the biologic systems, exergonic reactions, the energy from those is harnessed to allow endergonic reactions to take place.0436

In an exergonic reaction, energy would be released, and then, that energy is used to power endergonic reactions.0444

Systems overall tend towards lower free energy.0453

And looking outside of reactions in chemistry, looking at something as simple as a ball sitting on top of a hill, it has a higher potential energy, a higher free energy. It is less stable.0458

In order for it to go downhill, you are not having to input energy, it ends up at the bottom of the hill. It is more stable, and it is a lower free energy state.0470

Systems tend to want to go towards that lower free energy state.0480

Alright, if this cell is going to couple exergonic reactions with endergonic reactions, it has to have a means to do so.0486

It has to have a means to take that energy released by the exergonic reaction, and use it to power the endergonic reaction; and that means is through ATP.0494

ATP or adenosine triphosphate is what is called the energy currency of the cell.0504

It provides the direct source of energy for cellular processes.0510

An energy released from a chemical reaction could be used to form ATP, and then, ATP is broken down to release energy to power reactions that require the input of energy.0515

Let's look at how ATP stores energy.0530

Looking at the structure, what you have right here is a ribosugar, and here is the nitrogenous base adenine; and here, we have three phosphate groups.0533

The energy in ATP is stored in these bonds between the phosphate groups, and in particular, this third bond right here is the highest energy bond.0556

And the reason for that, the reason that there actually is energy stored in these bonds is because, look at the charge in the phosphate groups,0571

the phosphate groups have negative charges, but these light charges repel each other.0578

They do not want to be near each other, yet, these chemical bonds are holding the phosphate groups near each other.0586

And that is creating a high energy bond because the negative charge are repelling each other.0593

And these phosphate groups actually want to get away from each other, but they are forced together.0599

When this bond is cleaved, that stored energy is released.0604

When the terminal phosphate bond is hydrolyzed, energy is released, and that release of energy is in the form of this reaction.0608

The hydrolysis of ATP to form ADP, we would just have two phosphate groups on it plus Pi, and this is inorganic phosphate.0618

The ΔG under standard conditions of this reaction, is -7.3kcal/mol.0630

Hydrolysis of one ATP gives the cell about 7.3kcal/mol to use for processes such as0639

transporting certain substances into and out of the cell, repairing cell structures, growth, making proteins from amino acids.0651

All of these or almost all cellular processes are powered by ATP.0663

OK, where does the ATP come from?0671

In order to form ATP, the cell needs to take ADP - the reverse reaction of this - plus inorganic phosphate and form ATP, and that is going to require the input of energy.0673

That is an endergonic reaction. It has a ΔG of +7.3kcal/mol.0684

Well, cellular respiration, which we will go into in extreme detail in the next few lectures, provides the energy to form ATP.0692

Let’s look at the overall reaction for the breakdown of glucose.0703

Glucose C6H12O6 plus six oxygens will form six CO2 molecules plus six molecules of water.0707

The ΔG for this is -686kcal/mol.0720

When one molecule of glucose is hydrolyzed by the cell, the release of the energy will be -686kcal/mol.0727

And therefore, what you are going to end up with is six CO2s, plus six waters, plus some ATP,0737

which is where this energy is going to be stored, then, that ATP can go on to power other reactions.0743

Reactions like this that break down nutrients are called catabolic reaction- catabolic pathways.0749

Metabolic pathways can be divided up into catabolic, in which we have a breakdown of nutrients or molecules, and these release energy.0758

Anabolic pathways are the opposite.0775

Here, molecule are being combined or built, and here, that would require the input of energy.0778

These use energy. These will be endergonic reactions.0791

These are exergonic reactions.0794

For example, a cell could break down a molecule of glucose, release this energy, use that to form ATP, and then, the ATP could power an anabolic reaction0798

such as the formation of protein from amino acid monomers or polysaccharides, the creation of polysaccharides from monosaccharides, repair, building cell wall.0808

All of these what you are building up would be anabolic process.0822

Now, where does the cell get the glucose?0828

Well, for photosynthetic organisms like plants, glucose is made - in which we are going to talk about in a later lecture - using energy from sunlight plus some basic building blocks.0830

And glucose is formed and then, broken down.0844

In animals and organisms that do not undergo photosynthesis, nutrients need to be ingested and broken down, and then, that glucose is intracellular respiration pathway to release energy.0847

Alright, now we talked about energy, and we are going to get to where enzymes come into play.0865

Enzymes increase the rate of a reaction by lowering the active evasion energy required for the reaction to occur.0873

Remember that a spontaneous reaction, one with a -ΔG, it has an overall lower free energy in its final state than in its initial state.0880

However, you still may need to input some energy just to get the reaction started, but the overall change right here, we have reactants.0896

Here is the G of the reactants starting out, the free energy state right here, and then, here is a free energy of the products.0909

And if I look at the difference here, I take the G of the final state minus the G of the initial state.0919

In this reaction right here, it is going to be negative because the G of the final is lower than the G of the initial.0928

This is showing me the graph of an exergonic reaction.0937

Why do we need enzymes?0947

This is spontaneous reaction. It does not require the input of energy.0948

It will occur without the input of energy, but it may occur very, very slowly.0951

And in a cell, if a cell needs to break down glucose to release that energy, it cannot wait hours, week, several months, however long it would take for a reaction to occur.0958

A -ΔG tells me the reaction is spontaneous, but it could be very slow.0970

In order to speed up reactions, cells use enzymes. What enzymes are, are catalysts.0977

They increase the rate of the reaction but are not, themselves, altered by the reaction nor do they change the overall reaction that occurs.0984

Most enzymes are proteins.0994

Alright, before we go on, just to complete what we were discussing about exergonic reaction, just to make this clear, what would an endergonic reaction look like?0997

Well, let's say we started out here with some products, and we had the activation energy,1007

and then, the - excuse me - reactants started here then, the activation energy to get this going, and then, we ended up here with products.1015

Notice that the free energy G here of the products is higher than the free energy of the reactants.1028

If I measured the difference from reactants and products, I went ahead and I took OK, the G of the products minus the G of the reactants,1035

I would get a +ΔG because the products, the G is larger than the reactants.1048

This represents an endergonic reaction, and enzymes can catalyze either an exergonic or endergonic reaction.1058

For simplicity, we are going to focus here on exergonic reaction.1065

Now, as I said, it takes some energy to get the reaction going, and why is that?1068

Well, think about what a reaction is. It is breaking of chemical bonds and formation of new bonds.1076

Maybe you are taking a molecule of glucose and breaking those bonds and forming CO2 and water.1081

It takes energy to break the bonds, and to get the bonds in a position where they can break more easily, requires energy.1087

This state right here at the peak is what is called the transition state.1099

The input of energy to get to this transition state is called the activation energy Ea, so Ea is the activation energy.1107

It is the difference in the free energy between the reactants and the transition state.1117

We started here, some input of energy was needed to get this reaction going, to twist, turn, pull these bonds into a position where they will be ready to break.1126

Then, decrease in energy as the bonds break, and then, the new bonds are formed; and then, finally we get the products.1139

You can think of this as analogous to, let's say you are going to ride a bike.1151

You get on the bike, and you have to push extra hard to get the pedals moving; but once you are going, you do not have to pedal as hard.1156

It is the same idea here. Just to get things going, you need some energy input, and then, once they are moving, less energy required.1163

The uphill portion of this graph is what is called the activation phase. You get to the transition state, and then, the downhill part bonds are breaking and then, reforming.1171

Endergonic reaction, same idea, again, activation energy required to get to the transition state, and then, we have a downhill phase to get to the products.1184

How do enzymes work? How do they speed up reaction?1196

They do so by lowering the activation energy required.1199

Therefore, a reaction that is catalyzed by an enzyme might look something like this.1205

Notice that the blue one is catalyzed by an enzyme.1220

In fact, let’s even make this a little more dramatic. Let's lower the activation energy even more.1227

OK, notice that the activation energy, if I look right here, this Ea is smaller than the activation energy required for the uncatalyzed reaction.1236

Therefore, less energy is going to be needed to get this going, and the reaction will occur more quickly.1251

The ΔG has not changed.1259

If I look at where the reactants were, as far as free energy and where products are, as far as free energy- same for both the catalyzed and uncatalyzed reaction.1262

If I measure this difference- same. ΔG has not changed.1273

There is no change in the overall reaction. There is just a decrease in the activation energy required.1279

How do enzymes do this?1286

Well, what the enzymes do is that they hold the substrates in place in such a way that the bonds can more easily be broken, so some terminology first.1290

A substrate is the reactant that an enzyme acts upon, and you see it as enzyme specificity; and that is because enzymes are very specific for the reactions that they catalyze.1304

They can only catalyze reactions for certain substrates. They can only bind to very specific substrates.1315

Let's take a look at what is happening right here.1325

Here, we have the substrates or the reactants, and they are floating around; and what they do is they bind to the enzyme, and you see them bound here and formed.1327

This is the enzyme. This is what is called the enzyme substrate complex.1341

Binding occurs at what is called the active site.1355

This enzyme will only bind to the substrates that it is meant to bind to because of the shape of the active site.1364

And actually, the way this is drawn, it is very schematic, and it shows that this active site is already in a shape that will bind the substrates; but it is a little bit more complex than that.1372

Binding usually occurs by what is called an induced fit.1385

Induced fit means that the active site undergoes a conformational change once it comes into contact with the substrate.1389

Once the substrate or substrates come into contact with this enzyme, the active site will actually conform to fit really well.1397

It might start out, if you looked at it looking like it would not quite be the same shape.1407

It is not just like a puzzle piece that fits into a pre-cut puzzle board.1415

There is some change in the shape to allow the substrates to fit into the active site.1422

Binding occurs, and what the active site does is it holds the substrate or substrates in such a way that the bonds can break more easily.1428

The transition state, it moves the substrates toward that transition state. It might do it by twisting or turning or pulling.1440

The other thing it does is if there is more than one substrate, let's say instead of breaking down a molecule of glucose, we are going to form a molecule of glucose.1449

Then, the reactants, by putting them right next to each other, they are ready to collide and break bonds and reform new bonds.1458

After the reaction has occurred, the enzyme will release the reactants, the products - excuse me - the products.1469

Notice that the enzyme has not been changed.1478

It started out, bound to the reactants. Reaction occurs in the active site of the enzyme.1482

Products are released, and this enzyme is ready to go ahead and catalyze another reaction.1487

Therefore, you will only need a small amount of enzyme to catalyze many reactions.1493

As you come across enzymes in this course and in other courses, you will notice that often, they end in ase, and that is one way to recognize them for example lactase.1500

The ase tells me that it is an enzyme, and lac tells me what the substrate is. The substrate is lactose.1511

Lactase catalyzes the breakdown of lactose into the monosaccharides glucose and galactose, and you might have heard of lactose intolerance- people who cannot tolerate dairy products.1518

When they ingest dairy products their stomach gets upset. They get different GI symptoms.1536

And the reason is they are deficient in the enzyme lactase, and their body cannot breakdown lactose properly.1541

OK, we talked about how enzymes work, what they do. Now, we are going to discuss some factors that affect the activity of an enzyme.1550

There are multiple factors including the concentration of the substrate, temperature, pH and the presence or absence of cofactors.1560

Starting out with substrate concentration, at first, when you add more substrate, you will see that the reaction rate increases.1568

Adding more substrate, it makes sense that the reaction rate would increase because there might have been some enzyme sitting empty.1577

You add more substrate. Those enzymes bind to the substrate.1582

Reaction occurs. However, that only occurs to a point.1587

At a certain point, you can add more and more substrate, and yet, you see nothing else is happening.1590

The reaction rate is not increasing. The reaction rate just maxes out and stays steady, and that is because saturation has occurred.1596

Reaction rate increases by increasing the concentration of substrate until saturation is reached.1604

If you already have a lot of substrate, and all the enzymes are bound to substrate;1617

and there is more waiting there ready to go, dumping in a bunch more is not going to make things any faster.1623

It is just going to be a back log, so that is substrate concentration.1626

Enzymes also have what is called optimal conditions for their activity, and under optimal conditions, the rate of the reaction would be as fast as it could be.1631

And these conditions include temperature, pH and presence of cofactors.1643

Looking first at pH, this graph here, this shows a reaction occurring versus different pH, and you will see at these lower pHs, the reaction rate is not that fast.1648

But as the pHs increase, the reaction rate increases and increases and increases until it peaks at right around 7, approximately 7, so the optimal pH for this reaction is 7.1662

After that, if you continue to increase pH, make a more an alkaline environment, the reaction actually slows down.1676

The reaction rate slows down, and the reason is enzymes have an optimal pH that they function at; and outside of that pH, the enzyme may denature.1685

Remember that most enzymes are proteins and that denaturing means unfolding.1698

Proteins have a 3-dimensional conformation, and if the protein unfolds, then, the active site is going to change shape; and it is not going to bind to the substrate as well.1702

At certain temperature and pH, they are in optimal conditions. Outside of that, the enzyme does not function as well.1713

In humans, most enzymes function optimally at a pH of about 7, and this makes sense because the pH in our blood is about 7. However, that is not always the case.1726

For example, if you look in the stomach, the stomach has a very low pH.1738

The pH in the stomach is about 2-4, and if you look at an enzyme such as pepsin, it is going to function optimally at a lower pH.1741

Alright, that is pH. Now, temperature- same idea.1755

Increase in temperature up to a point will increase the rate of the reaction because the molecules are going to be moving faster, and then, they are more likely to collide.1759

Bonds are more likely to break, but once you get past the peak temperature, the rate of the reaction quickly drops off.1768

And again, that is because the protein becomes denatured or essentially melts at high temperatures.1774

In humans, optimal function of enzyme is at 37°C. That is our body temperature.1780

Above that, proteins may become denatured.1787

Below that, although, the enzyme will not denatured, the molecules just start moving as fast, and so the bonds are not as likely to be broken.1789

The final factor that we are going to discuss that can affect enzyme activity is the presence of cofactors.1797

Cofactors are molecules that certain enzymes require in order to function.1803

In order for the reaction to take place, of course, there needs to be the reactants. The enzyme will speed it up, and cofactors may be required.1809

An example of cofactors could be inorganic elements such as iron or copper ions.1819

There are also organic cofactors. These are usually called coenzymes.1827

These are organic cofactors. A major example is vitamins.1833

The importance of vitamins is that they act as coenzymes, and later, we will discuss some specific coenzymes.1841

They have different functions and different reactions, but an example would be acting as an electron acceptor for a reaction.1848

In order for the reaction rate to be as fast as possible, an enzyme needs to be under optimal conditions.1856

High substrate concentration, optimal temperature, optimal pH and necessary cofactors need to be available.1865

Now, if enzyme activity were not regulated, there would just be complete craziness in the cell because the cell might breakdown all this glucose, and the energy is not needed yet.1873

Or it might use up all its energy to make proteins that are not needed. Things would just be chaotic.1886

Obviously, the regulation of the reactions that occur in the cell is extremely important, and these reactions can be regulated by regulating the activity of the enzymes.1892

One way in which this regulation occurs is through inhibition, and there are two general types of inhibitors: competitive and non-competitive.1903

This is the figure I showed before, where it showed the enzyme, and there is a substrate and then, the enzyme substrate complex, the reactions occurring here at the active site.1912

And then, we have the enzyme again with the products.1925

Competitive inhibitors bind at the active site and compete with the substrate for binding.1934

Let's say I had this inhibitor, and it is a competitive inhibitor.1940

It shaped such that it can bind at the active site, and binding of this inhibitor to the active site would prevent binding of the substrate.1945

In that way the reaction is inhibited. Substrate cannot bind.1954

One thing to consider, though, is that it would be possible to overcome this inhibition by increasing the concentration of the substrate.1959

Let's say I had one molecule of inhibitor for every five molecules of substrate.1967

Well, that is going to significantly decrease the rate of the reaction.1975

However, if I put in lots more inhibitor, and I ended up with a thousand molecules of substrate for every molecule of inhibitor,1979

the effect to the inhibitor is going to be very small because there is just so much substrate there that the chances are the enzyme is going to bind with the substrate, not the inhibitor.1988

Competitive inhibition can be overcome by increasing the concentration of the substrate, so this is substrate concentration.1999

Non-competitive inhibition works much differently.2023

Competitive inhibitors bind at the active site. Non-competitive inhibitors bind to a site outside the active site.2028

They are not competing directly with the substrate for the site. Instead, they are binding elsewhere.2031

Let's say it is going to bind right here. OK, let's say I have a non-competitive inhibitor, and it binds here.2039

What this binding of a non-competitive inhibitor can do is cause that conformational change in the active site.2045

They cause a conformational change in the active site. They do not act directly on the active site.2053

They act indirectly, and this conformational change may cause the active site to have lower affinity or be less likely to bind with the substrate.2064

Two ways that inhibition can occur here: competitive, where the inhibitor literally competes with the substrate for binding at the active site, can be overcome by increase in substrate concentration.2073

Non-competitive inhibition: you can increase a substrate concentration as much as you want, and is not going to help because this inhibitor is not binding at the active site.2105

It is binding at another site, and once that site is bound, this is going to decrease the chance that substrate can bind to the active site because of the conformational change.2115

One particular type of inhibition is called feedback inhibition.2124

Feedback inhibition is very common in biology, and this is when the product or an intermediate of a pathway goes back and inhibits the reaction that formed it.2128

Let’s say I have a reaction where the reactants are A and B, and there is a series of steps.2146

It forms C, then, it forms D, and eventually I get to the products E and F.2156

With feedback inhibition, let's say E could go back and act as an inhibitor.2162

If this were the enzyme that catalyzes this reaction, maybe E acts as a non-competitive inhibitor and binds here2172

and then, prevents A and B, then, from binding to the active site by changing the conformation of the active site.2180

This is a great way for the cell to self-regulate because once a lot of E builds up, it will shut down this reaction so that resources are not wasted making more E.2186

Once the concentration of E drops, then, less inhibition will occur. A and B will react, and more E will be formed.2198

And an intermediate such as C and D could also be an inhibitor. It just depends on the particular pathway that you are looking at.2208

There is another type of regulator for enzymes called allosteric regulators, and allosteric regulators, maybe inhibitors, or they may be activators.2216

And these are regulators that affect an enzyme's activity through binding its sites outside of the active site.2226

I know that it is similar to what we talked about with non-competitive inhibitors, but this is slightly different.2232

The focus here is more on multi-subunit enzymes, so let's go ahead and discuss that.2238

This can be either inhibitors or activators.2244

A multi-subunit enzyme, let’s say there is four subunits - 1, 2, 3, 4 - and these multi-subunit enzymes often exist in an active form and another form that is the inactive form- slightly different shape.2253

What allosteric regulators do is they bind, and they stabilize the enzyme either in its active form or inactive form.2282

Let's say I have an activator shaped like this.2292

What this can do is go ahead and bind here and stabilize this enzyme.2303

It stays in that form. It is active.2310

It catalyzes the reaction.2313

Conversely, an inhibitor - let's say it is shaped like this - and it goes ahead and it binds right here and stabilizes the enzymes in its inactive form.2315

This is binding outside the active site, but it is stabilizing the enzyme in its active form.2330

Binding occurs. The reaction occurs.2341

Here, the opposite, the inhibitor is binding and stabilizing the enzyme in its inactive form.2342

Multi-subunit enzymes may also bind their substrates cooperatively.2352

Again, looking at this enzyme, let's say it is in its active form, and it has multiple subunits; and each of those subunits may happen to bind to a substrate,2358

and if that is the case, what sometimes happen is cooperative binding.2373

In cooperative binding, binding of the substrate - let's say this is the substrate to the first subunit - will make it easier for the second subunit to bind.2377

And that will make it easier for the third subunit to bind, and that will make it easier for the fourth subunit to bind.2386

Binding of one subunit to a substrate increases the affinity of the next subunit for the substrate. Binding is easier and so on.2392

A classic example of such cooperative binding is with hemoglobin.2401

Hemoglobin is found in red blood cells, and the job of red blood cell is to transport oxygen.2406

In hemoglobin there are actually four subunits.2411

Each of those subunits carries an oxygen molecule, and it has been found that binding of oxygen to the first subunit increases binding of oxygen to the second subunit and so on.2414

Hemoglobin is not an enzyme. It is just a carrier of oxygen.2426

I just want to point out that allosteric interactions are not limited to enzymes.2429

There can be this type of cooperative binding in other molecules as well.2434

In the case of an enzyme though, an allosteric interaction would involve a substrate usually because that is what an enzyme is doing- binding a substrate, catalyzing a reaction.2437

Alright, now, we are going to go ahead and focus on some examples.2451

The figure below depicts the graph of the reaction rate versus substrate concentration.2455

The orange line represents the graph when an enzyme is present without an inhibitor.2462

The blue line represents the graph for an enzyme with an inhibitor. Is the inhibitor competitive or non-competitive?2469

Looking at this first line, here, we have a reaction catalyzed by an enzyme.2477

Here, we have a reaction catalyzed by an enzyme, but there is an inhibitor present.2482

I noticed that as substrate concentrations increase, the rate of the reaction increases, increases, increases and then, levels off.2488

This would be, this point where it levels off is saturation.2498

Adding more and more substrate does not help once you get to saturation point.2503

Then, I look at the blue graph, and I see that at lower substrate concentrations, the reaction rate of this reaction is significantly lower than when the inhibitor is not present.2508

At this particular substrate concentration, I see for the uninhibited reaction, the rate is up here at the same substrate concentration, so this is no inhibitor- non-inhibited.2520

This is inhibited. Much lower rate of reaction is being inhibited.2539

However, as substrate concentration is increased, the difference in the rates between these two decreases and almost ends up same.2544

Increasing substrate concentration decreases the effect of the inhibitor.2558

Recall that competitive inhibitors bind to the active site of the enzyme, and they compete with the substrate.2578

Therefore, that type of inhibition can be overcome by increasing substrate concentration, and that is exactly what I see here.2585

Therefore, this is a competitive inhibitor.2592

Now, what would the graph look like for a non-competitive inhibitor?2598

Well, at first, if I added some substrate, it would increase the reaction rate because there has to be substrate around for the reaction to occur.2601

But then, I would see this graph level off way down here because this inhibitor is not being affected, no matter I put more substrate in- not helping.2611

I put more substrate in- not increasing because the inhibitor is not competing with the substrate. It is binding outside the active site.2625

This is uninhibited. This is enzyme with an inhibitor, and it showing the effect of increased substrate concentration at overcoming that inhibitor.2636

And finally, this is a competitive inhibitor and finally, non-competitive inhibitor.2645

What this blue line represents is the graph with an enzyme with a competitive inhibitor present.2650

Example two: thermophiles are microorganisms that live in very hot environments.2660

Which figure below depicts the graph of the activity for an enzyme found in a thermophile?2666

Each of these graphs shows reaction rate and temperature- reaction rate versus temperature.2673

Looking at the first one, the reaction rate increases as temperature increases as expected, and then, it peaks. It peaks at about 40°.2680

The optimal temperature for this reaction is 40°, which is probably the optimal temperature for the enzyme that catalyzed the reaction.2695

After that, the reaction rate drops off as the enzyme becomes denatured in warmer temperatures.2707

The second graph shows the reaction rate increasing and then, peaking, and that optimal temperature is a little more than 20, maybe 25 or so.2715

25°C is the optimal temperature for the functioning of the enzyme catalyzing this reaction.2725

And finally, over here, I see the rate of the reaction increasing and peaking at about 70°.2733

Knowing that this is a thermophile and that they live in very hot environments, I would expect the enzyme to function optimally at a warm temperature.2741

Therefore, this graph, the third graph, shows the graph that I would expect depicting the activity of an enzyme found in this type of organism.2751

For humans, the graph would look like this- the first one.2763

Example three: classify each reaction as exergonic or endergonic?2770

Remember that exergonic reactions release energy.2775

Endergonic reactions require an input of energy to take place.2779

This first reaction shows six CO2s plus six waters forming glucose plus oxygen.2784

This is the formation of glucose, and when a molecule is being formed, is being built, a more complex molecule, this is an anabolic reaction. It is therefore, endergonic.2792

The formation of glucose would require energy, so this first one is endergonic.2813

This next reaction shows the hydrolysis of ATP to ADP and inorganic phosphate. so this is showing the breakdown of ATP.2821

That third phosphate group is being removed, and that high energy bond is being broken, so that is going to release energy. Therefore, this is an exergonic reaction.2832

OK, here, again, I see glucose, now, plus six oxygens breaking down to form six CO2s plus six waters.2849

This is the reverse of the first reaction. Instead of the formation of glucose, which is an anabolic reaction, we have the breakdown of glucose.2863

This is a catabolic reaction. Therefore, this is also an exergonic reaction, so endergonic, exergonic, exergonic.2875

Down here, there are two molecules of glucose, and this is forming a molecule of maltose and water.2891

Again, we are building up a molecule. It is the formation of maltose from glucose monomers.2903

Since it is the formation, it is an anabolic reaction, and it is, therefore, endergonic.2915

This is an endergonic reaction. It is going to require the input of energy.2922

In the final example, example four, the graph below depicts energy versus reaction progress for a reaction with no enzyme present.2927

Sketch a graph that would represent the same reaction with the enzyme present.2939

We start out here with the reactants then, get to the transition state.2943

And the difference here in this energy, free energy, is the energy of activation then, the reaction occurs. Products are formed.2954

Notice that the free energy of the products is lower than the free energy of the reactants.2967

Therefore, this is actually going to have a -ΔG, and this is an exergonic reaction- just so some extra information.2978

Now, remember that enzymes lower the activation energy. They do not change overall ΔG.2986

What would I expect the catalyzed reaction to look like is something like this.2995

You have no way of knowing exactly how much the activation energy is - let's move this stuff out of the way - going to be lowered.3001

But you know that it will be lowered, and you would just ask for a sketch, so just the idea.3008

Now, the other thing that you know is that the ΔG is not going to be changed, so this is the reaction when enzyme is present.3013

The activation energy has been lowered. The original activation energy was that high.3026

The activation energy for the catalyzed reaction is just right here.3035

The ΔG, if I measure the G of the products minus the G of the reactants, is unchanged. I have not changed the reaction.3041

This shows the catalyzed reaction.3049

Thank you for visiting Educator.com, and I will see you again soon.3053

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