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Dr. Carleen Eaton

Dr. Carleen Eaton

Nucleic Acids and Proteins

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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 (32)

2 answers

Last reply by: Parsa Abadi
Mon Sep 11, 2017 4:10 PM

Post by Milad Owji on July 6, 2017

I am trying to get some help. The power points are all duplicated once you download them. It makes it hard to print them out. How can I get correct set of power point. I need these solve asap please

0 answers

Post by Peter Fraser on November 28, 2016

22:00:  I heard recently that sickle cell anaemia is a consequence of mutation which provides some resistance to malaria.

0 answers

Post by Joe Shmo on October 11, 2015

At about 0:56 of the lecture, I noticed that the 5' carbon is missing a hydrogen.

1 answer

Last reply by: Dr Carleen Eaton
Wed Jan 14, 2015 7:46 PM

Post by Anil George on December 30, 2014

In the titles of each sub section, under Nucleic Acids, cont., the word is spelled Pyridines, but during the lecture it is spelled pyrmidines. Which spelling is correct? Thank you

1 answer

Last reply by: Dr Carleen Eaton
Fri Apr 25, 2014 11:13 AM

Post by Beatrice Lim on April 21, 2014

Hi Dr. Eaton,

Just to clarify, are the alpha helices and beta pleated sheets formed from R-groups (side-chains) at all? Or are they only formed from hydrogen bonds between the carboxyl and amino groups on the polypeptide backbone? And are the tertiary structures formed purely from bonding of these R-groups? Thanks :)

1 answer

Last reply by: Dr Carleen Eaton
Wed Mar 26, 2014 6:39 PM

Post by Christian Benz on March 12, 2014

Hi Dr. Eaton
RNA isn´t always single stranded. There is also dsRNA.

0 answers

Post by Dr Carleen Eaton on August 27, 2013

Hi Eponine,

At a neutral pH of around 7, the side chain of Asparagine is uncharged (NH2). Basic amine acids such as lysine have charged side chains (e.g. NH3+).

1 answer

Last reply by: Dr Carleen Eaton
Tue Aug 27, 2013 6:25 PM

Post by Ikze Cho on August 25, 2013

Is the phosphate group in DNA negative?
Does it have 2 negatively charged Oxygens on it?

0 answers

Post by Eponine Rosner on August 15, 2013

I still don't understand why asparagine is not basic. I know that the amino group is bonded to the carbonyl group, but why does that make it polar instead of basic?

1 answer

Last reply by: Dr Carleen Eaton
Mon Aug 19, 2013 3:55 PM

Post by Grace Gu on August 15, 2013

Can a side chain be both polar and acidic or polar and basic?

1 answer

Last reply by: Dr Carleen Eaton
Mon Aug 19, 2013 3:55 PM

Post by Grace Gu on August 14, 2013

I don't know if it's the problem of my internet or this video. The video always stops at amino acids and polypeptides and it always goes back to the beginning whenever I fast forward.

1 answer

Last reply by: Dr Carleen Eaton
Mon Aug 19, 2013 3:53 PM

Post by Grace Gu on August 14, 2013

Hi Dr. Eaten,

  You said that in order to distinguish the carbons on the nitrogenous bases from the atoms of the sugar, the atoms on the sugars, ribose and deoxyribose, have a prime after them? Like 2' and 3' and those refer to the different atoms on the sugar? How exactly does that work? How do you actually distinguish them?

Thank you!

0 answers

Post by sushant komawar on October 20, 2012

Hi,

How many tetrapeptides could be formed from four different amino acids?

1 answer

Last reply by: Dr Carleen Eaton
Tue Aug 27, 2013 5:52 PM

Post by Suresh Sundarraj on August 5, 2012

Dr Eaton,
I didn't quite understand what 5' and 3' ends are.
Thanks

1 answer

Last reply by: Dr Carleen Eaton
Thu Jun 21, 2012 12:23 PM

Post by Vagisha Joshi on June 6, 2012

A big big thanks...I love the way you teach.

1 answer

Last reply by: Dr Carleen Eaton
Tue Apr 3, 2012 5:48 PM

Post by Marcus Lind on April 1, 2012

Hi,

Which is the most common 3-dimensional structure of DNA? Name four structural criteria you can use to recognize it. Give an example of a
alternative DNA structure and indicate how it differs from the normal structure.

Thanks

0 answers

Post by Ioana Anastasescu on October 2, 2011

I know that you covered the structures of the proteins, but what about the Motifs and Domains?

2 answers

Last reply by: Billy Jay
Fri Apr 8, 2011 12:46 PM

Post by Billy Jay on April 8, 2011

Aren't hydrophobic interactions the same exact thing as London Dispersion Forces (Van der Waals)? I know you mention "Hydrophobic Interactions" as it's own distinct force to explain the hydrophobic nature of non-polar molecules (water fearing), but they're essentially the same thing.

Nucleic Acids and Proteins

  • Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) are polymers composed of nucleotides.
  • Nucleotides consist of a nitrogenous base, a pentose (5 carbon sugar) and a phosphate group. The sugar found in RNA is ribose, the sugar found in DNA is deoxyribose.
  • There are two groups of nitrogenous bases: pyrimidines - cytosine (C), thymine (T) and uracil (U) and purines – adenine (A) and guanine (G). RNA contains uracil whereas DNA contains thymine.
  • Two complementary strands of DNA pair up to form a double helix.
  • Amino acids are the building blocks for proteins. Each has an asymmetric carbon atom bonded to an amino group (NH2) a carboxyl group (-COOH) a hydrogen atom and a side chain called an R group.
  • Amino acids join together through the formation of peptide bonds to form polypeptides.The primary structure of a protein is the amino acid sequence in its polypeptide chain.
  • The secondary structure of a protein is a result of hydrogen bonding between different regions of a polypeptide chain. Alpha helices and beta pleated sheets are the two major types of secondary structure.
  • The tertiary structure is the overall three dimensional shape of the protein. Quaternary structure refers to the structure formed when multiple polypeptide chains interact to form a single protein.

Nucleic Acids and Proteins

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
  • Nucleic Acids 0:09
    • Deoxyribonucleic Acid (DNA) and Ribonucleic Acid (RNA)
  • Nucleic Acids, cont. 2:56
    • Purines
    • Pyrimidines
  • Double Helix 4:59
    • Double Helix and Example
  • Proteins 12:33
    • Amino Acids and Polypeptides
    • Examples: Amino Acid
  • Polypeptide Formation 18:09
    • Peptide Bonds
    • Primary Structure
  • Protein Structure 23:19
    • Secondary Structure
    • Alpha Helices and Beta Pleated Sheets
  • Protein Structure 25:43
    • Tertiary Structure
    • 5 Types of Interaction
  • 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

Transcription: Nucleic Acids and Proteins

Welcome to Educator.com.0000

We are going to continue our discussion of large biological molecules with a lesson on nucleic acids and proteins.0002

In the previous lecture, we talked about two other classes of large biological molecules- carbohydrates and lipids.0010

I also introduced some basic sub-organic chemistry there, so if you have not watched that lecture yet,0017

and you are not familiar with organic chemistry, you may want to watch at least the first part of that before going on to this.0022

There are two types of nucleic acids: DNA/deoxyribonucleic acid and ribonucleic acid.0030

DNA contains an organism's genetic information, and that information is passed on from parents to offspring.0037

DNA codes for proteins.0045

In the molecular biology section, we will talk about how DNA is synthesized, how the DNA is transcribed into RNA, and how that RNA is translated into a protein.0048

Right now, we are just focusing on the structure of both DNA and RNA.0062

DNA is made up of nucleotides. These are the building blocks for the DNA molecules.0068

RNA, same thing, it is made up of monomers of nucleotides, so let's go ahead and look at the nucleotide structure.0078

There are three parts: there is a sugar; there is a nitrogenous space; and there is a phosphate group.0087

In both DNA and RNA, the sugars are 5-carbon sugars, so these are pentoses.0096

However, the sugar in DNA is deoxyribose, whereas RNA contains ribose, so the name explains the difference.0102

Deoxyribose is missing one of the oxygens, so ribose has a hydroxyl group here, whereas DNA just has a hydrogen.0111

That is one difference between DNA and RNA although their fundamental structure is the same.0124

DNA and RNA both have nitrogenous bases attached to the sugars, and there are five different types of nitrogenous spaces that we will look at in the next slide.0131

If you just consider the nitrogenous base plus the sugar in either DNA or RNA, that is called the nucleoside.0147

With the phosphate group added, you have a nucleotide.0158

These nucleotides are the monomers from which the larger DNA or RNA molecule are formed.0168

Here, are shown the five different nitrogenous bases, and they can be classed into two groups.0182

These first two are more complex. They have a 6-membered ring fused to a 5-membered ring, and these are known as purines.0192

These top two are purines, and there are two.0202

Adenine, it is often known by its abbreviation A and quinine known by just the letter G.0205

Here, below in this row, are the pyrimidines. They are based on this 6-membered ring.0213

And these are rings that contain carbon and nitrogen, and there are three pyrimidines: cytosine, thiamine and uracil.0221

One important thing to know is that thiamine is found only in DNA, whereas uracil is found only in RNA.0231

In lieu of thiamine, RNA has uracil, otherwise, DNA and RNA have the same nitrogenous bases.0245

A, G and C are found in both DNA and RNA, thiamine only in DNA, uracil only in RNA.0255

One thing also to keep in mind as you are looking at structures of RNA and DNA is that in order to distinguish the carbons0262

on the nitrogenous bases from the atoms on a sugar, the atoms on the sugars - ribose and deoxyribose - have a prime after them.0272

So, we will sometimes be referring to the 2-prime or the 3-prime carbon, and those refer to the different atoms on the sugar.0282

These prime means that we are talking about the atom on the sugar versus an atom on these nitrogenous bases.0292

Nucleotides join to form polymers that consist of a sugar phosphate backbone with the attached nitrogenous bases.0301

One nucleotide is linked to the next nucleotide to form what is called a polynucleotide.0310

The monomers are the nucleotides, and they join to form polynucleotides; and that is usually what we are talking about when we talk about DNA and RNA.0317

The linkage that attaches these is known as a phosphodiester linkage.0326

Remember, when you just looked at the monomers, each one of them had a sugar, a nitrogenous base and a phosphate group.0342

And the phosphate groups serve as the linkage between one monomer and the next monomer.0348

We are going to talk about this synthesis in detail in the molecular biology lecture, but for right now, you should be aware that there is a directionality to DNA.0357

And we discussed DNA and RNA as having 5-prime ends and 3-prime ends.0365

The 5-prime carbon on what we call the 5-prime end of the polynucleotide has a phosphate group attached, so this is the 5-prime end.0375

There is a phosphate group attached to the 5-prime carbon.0385

This end is called the 3-prime end, so there is this three hydroxyl group.0392

Here, we have this phosphate group to 5-prime end, and then, we have the hydroxyl group attached to a 3-prime carbon on the 3-prime end.0400

This directionality is very important because synthesis of DNA always occurs 5-prime to 3-prime.0409

And again, we will get into the details of that later, but right now, you should just know the basics that there is a 5-prime end. There is a 3-prime end.0417

Two adjacent nucleotides are linked via a phosphodiester linkage.0424

And you should also be aware that this section, the sugar and the phosphate group, are known as the sugar-phosphate backbone,0430

so, sugar-phosphate backbone right here and then, attached nitrogenous bases.0442

The order of these nitrogenous bases is the genetic code.0452

You could have a strand of DNA that may have a nitrogenous base A attached. The next one is G, then another G, C, T.0458

And it is these bases, it is the order of those bases, that encodes the information to make a protein.0468

And it is this information, this order of the bases, that is passed along from parent to offspring.0475

DNA is found in a double helix structure. This double helix structure is formed by two complimentary strands.0483

These strands are also anti-parallel, so what do we mean by anti-parallel? Well, it has to do with that directionality.0491

Let's say that this is the 5-prime end of one of these pieces of DNA, and we follow this down; and it is going to end here at the 3-prime end.0501

The other strand is going to have the opposite orientation where it starts with the 3-prime end up here and then, ends at the 5-prime end down here.0512

So, we say that these two strands are anti-parallel. They are complimentary, and they are anti-parallel.0522

The 5-prime to 3-prime versus 3-prime to 5-prime explains the anti-parallel.0532

What does complimentary mean? Well that has to do with what is called base pairing.0538

Remember that in DNA, there is no uracil used. We have A, G, C and T.0542

Adenine pairs with thiamine, and this would be called a base pair; and G/guanine pairs with cytosine.0553

Here is a sugar-phosphate backbone shown with a purple.0572

And then, the nitrogenous bases A, G, C and T actually stick inward towards the center, towards the middle of this double helix.0575

This double helix structure was actually a famous discovery by Watson and Crick in the 1950s.0594

And, we have the sugar-phosphate backbone, and then, let's say this nitrogenous base here is A and T, C, G, A, T.0600

Since A pairs with T, this complimentary strand is going to have a T.0619

T pairs with A. The complimentary strand will have a an A.0624

C is going to pair up with G, so you are going to have a G here.0627

G, C, A pairs up with T. T pairs up with A and so on.0635

Complimentary refers to the fact that the base pair on the second strand matches with the base on the first strand.0643

Now, hydrogen bonding occurs between these base pairs, and that is what holds this helix in its structure.0655

And you will notice up here that I showed three dotted lines between G and C, whereas there is only two dotted lines between A and T.0663

And that is because A-T forms two hydrogen bonds with each other, whereas G and C form three hydrogen bonds with each other.0671

OK, important place to remember is that DNA is a 5-prime end, a 3-prime end.0681

Nucleotides are linked by a phosphodiester linkage.0686

Their structure is such that there is a DNA double helix that is formed between two complimentary anti-parallel strands.0691

Each strand is paired so that it has a matching base pair.0702

A always pairs with T. G always pairs with C.0709

And these nitrogenous bases, these base pairs, form hydrogen bonds that keep this double helix structure in place.0714

RNA is single-stranded.0723

In biology, form follows function, and you will see how this double helix is very important0731

in the synthesis of DNA and in producing DNA that has as few mistakes as possible, so that genetic mistakes or mutations are not introduced.0735

We will revisit this double helix structure later on with a focus on DNA synthesis, transcription and translation.0744

The next large biomolecule that we will talk about is proteins.0755

Amino acids are the building blocks of proteins, and these join to form polypeptides.0759

So, remember that DNA contain genes, and these genes encode proteins.0765

Proteins are extremely important to living organisms because they make up structural elements such as our muscles.0773

They facilitate reactions in the form of enzymes, which we will discuss later.0781

They are involved in cell signalling. They are involved in cell growth and the repair of cells, so proteins are fundamental to life.0785

There are twenty main or common amino acids.0792

You do not have to know each of these. You just need to know the general structure of amino acids and some different classifications of the amino acids.0797

Let's look at just a generalized amino acid. You are going to see that it has certain groups.0805

Here, it has an amino group. On the other side, it has a carboxyl group.0810

In the center is a carbon atom, so bonded to the carboxyl group, the amino group, a hydrogen and then, what we call an R-group.0821

The R-groups are different, so each of the twenty amino acids has a different R-group.0830

It could be as simple as just hydrogen. That would be just glycine, structurally the simplest amino acid.0836

Or it could have more complex functional group like shown here with asparagine or even more complex than that.0839

You might see amino acids also written instead of NH2, you might see this shown as NH3+ and the carboxyl group as COO-.0852

And that is because in water, the amino group picks up a hydrogen ion and, therefore, acts as a base.0862

And that carboxyl group loses a hydrogen ion and, therefore, acts as an acid.0871

You are also going to notice that there are 3-letter abbreviations for the amino acids, so you might see instead of asparagine written out, Asn.0880

Or for example, leucine is another amino acid that is abbreviated as Leu and glutamine, Gln.0888

There are also 1-letter abbreviations for the amino acids.0896

Let's talk a little bit more about these side chains. The side chains can be grouped such that they are non-polar, they are polar, they are acidic, or they are basic.0900

First, let's just talk about non-polar.0926

Glycine has an R-group that is just a hydrogen atom. That is going to be an example of a non-polar amino acid.0929

A polar amino acid might have, for example, hydroxyl groups on it or some other polar functional groups.0941

Asparagine is actually considered a polar amino acid, so this one is polar.0950

Acidic and basic are a little bit more complicated.0957

When we talk about acidic or basic amino acids, we are not talking about the amino group here or the carboxyl group here.0960

We are talking about the R-group or the side chain.0966

If you think about it, in a solution, this is going to pick up a hydrogen ion. This is going to lose one.0970

They are going to essentially neutralize each other.0974

So, the amino acids overall, in the different forms that they are in in solution. If they are not, it is going to be that they are neutral.0976

However, if there is a carboxyl group on the side chain, if the side chain has a carboxyl group, then, you would have an acidic amino acid.0985

If the side chain contains an amino group, then, you would have a basic amino acid.0998

Again, we are not looking at this. When we talk about polar or non-polar amino acids, we are talking just about what is going on with the side chain.1008

I want to point this out. This is a bit of an exception.1015

Glutamine and asparagine are both polar. They are not basic.1020

Even though you see this NH2 here, and you might think "oh, an amino group".1027

This particular construction, where you have C double bonded to O, linked to NH2, is something called an amide group.1030

And this is a bit different. It is not actually basic.1039

If you had this NH2 but it was not linked to the C double bond O, then, I would say "OK, you have a basic amino acid".1044

But this particular group together actually is not a basic side chain.1049

Glutamine has this group. Asparagine has this group.1055

These two are classed as polar, not as basic.1058

Aspartic acid is a good example of an acidic amino acid. The side chain contains COOH, this carboxyl group and that cellular pH.1063

This becomes ionized to COO-, and therefore, this is an acidic amino acid. It tells you so in its name.1079

OK, we talked about amino acids. These are the building blocks for proteins.1089

Amino acids can be joined together to the formation that is called a peptide bond.1095

A peptide bond is yet another dehydration reaction.1101

We discussed that in previous lecture where a dehydration reaction is a reaction where water is removed, so we lose a water.1104

Recall that the basic structure of an amino acid would be NH2, central carbon, an R-group, hydrogen, and then, we have this carboxyl group, COOH.1115

An adjacent amino acid would have the same structure, so now, we are just going to do COOH over here, R here.1139

Here, we have the NH2, and here we have H; so, let's write this as NHH1150

This peptide formation, again, is through a dehydration reaction, so water is going to be lost.1163

So, if an OH is removed from here, and then, H is removed from here, you are going to end up with H2O removed.1169

And that will leave this CO, which is this, becomes double bond, and this nitrogen, which is here, bonded together.1179

This carbon from the carboxyl group bonds to the nitrogen from the amino group, and water is lost.1189

Again, COOH and NH2, loss of an OH group from the carboxyl, a hydrogen from the amino group, leaving behind C double bonded to O.1195

And then, the C bonds to the nitrogen and then adjacent amino acid forming a peptide bond.1206

What is shown here is a dipeptide. It is two amino acids.1213

Three or more amino acids are a polypeptide chain, and a polypeptide chain can be very short, just a few amino acids.1216

It can be a thousand amino acids long.1223

The primary structure of a protein is the amino acid sequence of its polypeptide chain.1226

There are multiple levels of structure in a protein. There are three to four depending on the type of protein: primary, secondary, tertiary and quaternary.1233

The primary structure is just the order of the amino acids if it is leucine and glycine, glutamic acid, then another asparagine, another asparagine.1242

That would be giving the primary structure of the protein.1252

Now, polypeptides are not the same as proteins. Polypeptides are just chains of amino acids.1259

They are in a particular order, but if they are unfolded, they are just chains- they are polypeptides.1268

In order to actually be protein, a polypeptide chain or chains - sometimes there is more than one chain in the protein - need to be folded1273

in a unique 3-dimensional conformation, then, that is a protein.1280

Once you just have bunch of amino acids linked, it is not a protein yet. It is a protein once it is folded.1285

The primary structure is actually what determines this folding, although nobody is quite sure how.1291

And the primary structure of a protein was first elucidated by Fred Sanger at Cambridge, and he and his lab actually sequenced insulin.1298

Remember that insulin is a hormone secreted by the pancreas, and it is vital in controlling glucose levels in the bloodstream.1308

Without enough insulin, a person becomes diabetic.1315

Another medical example of the importance of the primary structure of protein is the disease sickle-cell anemia.1317

This disease is caused by the substitution of a single amino acid- valine.1327

Instead of valine, it is actually, valine is substituted for glutamic acid, so valine substitution.1334

That change of that one amino acid to a different amino acid causes problems in the structure of hemoglobin.1347

Hemoglobin is found in red blood cells. It carries oxygen.1355

The structure of the hemoglobin is abnormal in people with sickle-cell anemia, and the result is that it actually causes the red blood cells to form a sickle shape.1359

And those sickle-shaped cells tend to clump up.1367

Red blood cells are normally a biconcave disk. They move nicely through even small vessels like capillaries.1373

With sickle-cell anemia, these cells form a sickle shape. They clump up, and that causes poor circulation to various parts of the body and symptoms.1379

The primary structure of a protein is very important in determining the secondary and tertiary structure and the function of the protein.1388

So, we went to this first level of structure. Let's go into more detail about the other levels1397

The secondary structure of a protein is the result of hydrogen bonding between different regions of the polypeptide backbone.1402

When I say polypeptide backbone, that means not the side chain. It means the other parts.1409

The two main protein secondary structures are alpha-helices and beta-pleated sheets, so let's go back to how these are formed.1415

There are certain regions on a polypeptide strand that are repeated, and particular repeated regions allow for hydrogen bondings.1424

This bonding occurs between the electronegative oxygen atoms and the hydrogen atoms attached to the nitrogen.1434

So, remember your basic amino structure. There is an R-group.1450

There is a carboxyl group. There is hydrogen, and there is an amino group.1454

And the hydrogen on the amino group is attracted to the electronegative oxygen atoms in these carboxyl groups.1460

This would cause hydrogen bonding between one amino acid and another nearby amino acid.1468

We are not talking about the side chains. We are just talking about the backbone structure, which is this part.1475

The electronegative oxygen and a hydrogen atom attached to a nitrogen can form hydrogen bonds.1482

If there are certain repeated regions, particular types of repeated regions, you can end up with either this helix shape - it is like a spiral -1491

or what is called a beta-pleated sheet, and it is like if you took a piece of paper or something and folded it up.1503

So, this is the alpha-helix and beta-pleated sheet.1509

The important thing to remember about secondary structure is that the hydrogen bonding is between the polypeptide backbones, not the side chains.1521

And that the two main types of secondary structures are alpha-helices and beta-pleated sheets.1528

Again, one hydrogen bond is not that strong, but many hydrogen bonds together could hold the structure in place and stabilize it.1534

The next level of structure is tertiary structure, and tertiary structure is the overall 3-dimensional shape of the protein.1545

This shows a protein that might be described as a globular protein. It is shaped like a globe.1554

An example would be hemoglobin.1561

Within this overall 3-dimentional or tertiary structure, certain regions may have an alpha-helix.1568

Maybe this region over here is beta-pleated sheet, and this is beta-pleated sheet; and this is neither.1575

And then, there is another alpha-helix here and here.1582

The entire polypeptide does not usually form one big alpha-helix or beta-pleated sheet.1585

Often, there is just little regions of each in certain areas of the protein, and then, those regions, along with the rest of the protein, fold into a unique shape.1591

And the shape is extremely important to the protein's function.1603

When we talk about enzymes, you will see that the shape of the enzyme is crucial in it being able to facilitate a reaction.1606

There are five types of interactions that form and maintain the tertiary structure.1617

The first one is hydrogen bonding, but this time, it is of those side groups.1630

Remember that hydrogen bonding between a main polypeptide backbone will form secondary structures such as alpha-helices and beta-pleated sheets.1640

Those amino acids that contain hydroxyl groups or amino groups, for example, can hydrogen bond and help to stabilize the 3-dimensional structure.1648

The second type of bond is ionic bonds.1662

Remember that there are certain charged side groups.1665

We talked about the fact that there are some amino acids that are acidic and some that are basic.1670

So, those are charged, and they can form ionic bonds with each other.1675

The third type is known as a disulfide bridge.1679

Cysteine is an amino acid that contains SH on its side chain.1688

Two cysteine molecules can each lose a hydrogen and form what is called a disulfide bridge or bonds.1694

If I have two cyteins near each other, and they each lose a hydrogen; and they form this disulfide bridge or disulfide bond.1705

And this is a covalent bond, but it is still a crucial in forming the tertiary structure.1712

The fourth type is hydrophobic interactions, and what this refers to is that non-polar or amino acids with1719

non-polar side chains often end up clustered in the central part or in the middle of the protein structure.1732

And this is because those amino acids that have polar side chains can form hydrogen bonds with water.1740

So, when proteins are in a solution, the side chains that are polar interact with the water molecules.1746

They form hydrogen, and then, the non-polar ones pretty much just end up excluded from that and pushed to the center.1752

And when these non-polar ones are near each other, they can form various bonds and non-polar interactions.1758

There is one type of interaction between non-polar molecules that are called Van der Waal reactions.1765

These are another type of weak bond, and these form between non-polar molecules.1774

Again, the tertiary structure is the overall shape of the protein. It involves bending and folding.1781

And there are five types of interactions that form and maintain the tertiary structure: hydrogen bonding between the side groups,1787

ionic bonds between side groups that are charged, disulfide bridges between cysteine molecules, hydrophobic interactions, and finally, Van der Waals interactions.1796

There is one final level of structure only for certain proteins, and this is quaternary structure.1807

There are certain proteins that are formed from more than one polypeptide chain.1813

And the interaction between multiple chains in a multi-subunit protein is known as quaternary structure.1817

An excellent example is hemoglobin. Hemoglobin has four polypeptide chains that form the four sub-units of hemoglobin.1823

And not only does each of these chains have a certain tertiary structure,1833

but all four of the chains come together in an overall structure known as a quaternary structure.1837

When you think about protein folding, you need to be aware that certain conditions affect folding.1844

There is an optimal temperature for the folding of proteins. There is an optimal pH and osmolarity or salts concentration.1849

If for example temperature is changed, if a protein is heated up, it melts or unfolds, and we call this "denatures".1861

When a protein denatures, it means that it unfolds.1871

If the pH is changed, if you take a solution and add a bunch of salt to it, the proteins in it could also denature.1875

Proteins function optimally at certain conditions depending on that protein.1882

Like in our bodies, the pH, most areas of our body is about 7.4, so most of the proteins in our body function best at that pH and at our body temperature.1888

If a protein denatures, since formed for all those function, it is not going to function very well.1898

Now, let's go ahead and review some examples focusing on nucleic acids and proteins.1905

Write the complimentary strand for a strand of DNA with the following sequence.1911

Alright, this shows the 5-prime end and the 3-prime end, and then, it shows a sequence G-C-C-A-G-T-T-C-A-A-G for DNA, so, this is at different nitrogenous bases.1917

The first thing in a question like this is to remember that the two strands are anti-parallel.1932

So, right away, as part of the answer, you should always write in the 3-prime and the 5-prime, and they are going to be opposite because it is anti-parallel.1936

The strand is going to be anti-parallel and complimentary.1944

Remember that G forms three hydrogen bonds with C, and A forms two hydrogen bonds with T; so these are the ones that pair up.1948

Therefore, when there is a G, it is going to pair up with the C. A C will pair up with the G, again, with the G.1960

Here, I have an A. It pairs with T.1967

G pairs with C. 2 Ts, these each pair with A.1970

C pairs with G. As pair with T and finally, G and C, so the complimentary strand is going to be 3-prime to 5-prime.1975

The Gs will be paired with Cs. Cs will be paired with Gs.1985

A and T go together and T and A.1989

This is the complimentary strand for this strand of DNA.1993

Example 2: list two differences between DNA and RNA.2001

Well, recall that RNA contains uracil. DNA contains thiamine- that is one difference.2006

Second difference: RNA is single-stranded. DNA is double-stranded.2023

And they only ask for two, but the third difference is that the sugar for RNA is ribose, whereas the sugar for DNA is deoxyribose.2040

Here is three differences. Any two would have sufficed to answer the question: difference in nitrogenous bases,2061

single versus double-stranded and ribose sugar versus deoxyribose sugar.2067

Is each of the following amino acids polar, non-polar, acidic or basic?2076

To determine that, remember you are just going to look at the side chains, the side chains right here, here and this whole region here.2080

I am not going to pay attention to this carboxyl or amino group that is present on the backbone.2090

Right here, this is the simplest amino acid - I mentioned before - which is glycine, and glycine is non-polar. It just has a hydrogen.2098

This second amino acid is serine. Serine, you see, has a hydroxyl group, which is polar, so this is a polar amino acid.2109

Lysine is a little bit more complicated, and you will notice that it has an amino group.2120

When this is put in solution, this amino group is going to pick up a hydrogen ion and become NH3+. Therefore, it is basic.2126

We have three amino acids, three different categories: non-polar hydrogen side chain, serine is polar with a hydroxyl group,2135

and finally lysine, which is a basic amino acid.2142

List four types of interactions that maintain the tertiary structure of a protein.2148

The first one is hydrogen bonding, and remember that this is hydrogen bonding between the side groups or the R-groups, not between the backbone.2154

Second type is hydrophobic interactions.2169

These occur as a result of amino acids with hydrophobic side chains being pushed towards the center of the2175

protein being excluded from the hydrogen bonding of water and the polar side chains of some of the other amino acids.2182

These are hydrophobic interactions.2188

A type of weak interaction between non-polar side chains is called Van der Waals interactions.2191

If there are some cysteine containing amino acids that are cysteine, they contain sulfur,2203

then, there may also be disulfide bridges that help to maintain this tertiary structure.2210

This was four, but a fifth one is ionic bonds between amino acids that are charged.2218

So, here is five. Any four of these would answer the question of the four types of interactions that maintain the tertiary structure of a protein.2231

That concludes this lecture on Educator.com.2239

Thanks for visiting.2242

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