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Boundless Biology: 15.5: Ribosomes and Protein Synthesis

Boundless Biology
15.5: Ribosomes and Protein Synthesis
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table of contents
  1. 1: The Study of Life
    1. 1.1: The Science of Biology
      1. 1.1.0: Introduction to the Study of Biology
      2. 1.1.1: Scientific Reasoning
      3. 1.1.2: The Scientific Method
      4. 1.1.3: Basic and Applied Science
      5. 1.1.4: Publishing Scientific Work
      6. 1.1.5: Branches and Subdisciplines of Biology
    2. 1.2: Themes and Concepts of Biology
      1. 1.2.0: Properties of Life
      2. 1.2.1: Levels of Organization of Living Things
      3. 1.2.2: The Diversity of Life
  2. 2: The Chemical Foundation of Life
    1. 2.1: Atoms, Isotopes, Ions, and Molecules
      1. 2.1.0: Overview of Atomic Structure
      2. 2.1.1: Atomic Number and Mass Number
      3. 2.1.2: Isotopes
      4. 2.1.3: The Periodic Table
      5. 2.1.4: Electron Shells and the Bohr Model
      6. 2.1.5: Electron Orbitals
      7. 2.1.6: Chemical Reactions and Molecules
      8. 2.1.7: Ions and Ionic Bonds
      9. 2.1.8: Covalent Bonds and Other Bonds and Interactions
      10. 2.1.9: Hydrogen Bonding and Van der Waals Forces
    2. 2.2: Water
      1. 2.2.0: Water’s Polarity
      2. 2.2.1: Water’s States: Gas, Liquid, and Solid
      3. 2.2.2: Water’s High Heat Capacity
      4. 2.2.3: Water’s Heat of Vaporization
      5. 2.2.4: Water’s Solvent Properties
      6. 2.2.5: Water’s Cohesive and Adhesive Properties
      7. 2.2.6: pH, Buffers, Acids, and Bases
    3. 2.3: Carbon
      1. 2.3.0: The Chemical Basis for Life
      2. 2.3.1: Hydrocarbons
      3. 2.3.2: Organic Isomers
      4. 2.3.3: Organic Enantiomers
      5. 2.3.4: Organic Molecules and Functional Groups
  3. 3: Biological Macromolecules
    1. 3.1: Synthesis of Biological Macromolecules
      1. 3.1.0: Types of Biological Macromolecules
      2. 3.1.1: Dehydration Synthesis
      3. 3.1.2: Hydrolysis
    2. 3.2: Carbohydrates
      1. 3.2.0: Carbohydrate Molecules
      2. 3.2.1: Importance of Carbohydrates
    3. 3.3: Lipids
      1. 3.3.0: Lipid Molecules
      2. 3.3.1: Waxes
      3. 3.3.2: Phospholipids
      4. 3.3.3: Steroids
    4. 3.4: Proteins
      1. 3.4.0: Types and Functions of Proteins
      2. 3.4.1: Amino Acids
      3. 3.4.2: Protein Structure
      4. 3.4.3: Denaturation and Protein Folding
    5. 3.5: Nucleic Acids
      1. 3.5.0: DNA and RNA
      2. 3.5.1: The DNA Double Helix
      3. 3.5.2: DNA Packaging
      4. 3.5.3: Types of RNA
  4. 4: Cell Structure
    1. 4.1: Studying Cells
      1. 4.1.0: Cells as the Basic Unit of Life
      2. 4.1.1: Microscopy
      3. 4.1.2: Cell Theory
      4. 4.1.3: Cell Size
    2. 4.2: Prokaryotic Cells
      1. 4.2.0: Characteristics of Prokaryotic Cells
    3. 4.3: Eukaryotic Cells
      1. 4.3.0: Characteristics of Eukaryotic Cells
      2. 4.3.1: The Plasma Membrane and the Cytoplasm
      3. 4.3.2: The Nucleus and Ribosomes
      4. 4.3.3: Mitochondria
      5. 4.3.4: Comparing Plant and Animal Cells
    4. 4.4: The Endomembrane System and Proteins
      1. 4.4.0: Vesicles and Vacuoles
      2. 4.4.1: The Endoplasmic Reticulum
      3. 4.4.2: The Golgi Apparatus
      4. 4.4.3: Lysosomes
      5. 4.4.4: Peroxisomes
    5. 4.5: The Cytoskeleton
      1. 4.5.0: Microfilaments
      2. 4.5.1: Intermediate Filaments and Microtubules
    6. 4.6: Connections between Cells and Cellular Activities
      1. 4.6.0: Extracellular Matrix of Animal Cells
      2. 4.6.1: Intercellular Junctions
  5. 5: Structure and Function of Plasma Membranes
    1. 5.1: Components and Structure
      1. 5.1.0: Components of Plasma Membranes
      2. 5.1.1: Fluid Mosaic Model
      3. 5.1.2: Membrane Fluidity
    2. 5.2: Passive Transport
      1. 5.2.0: The Role of Passive Transport
      2. 5.2.1: Selective Permeability
      3. 5.2.2: Diffusion
      4. 5.2.3: Facilitated transport
      5. 5.2.4: Osmosis
      6. 5.2.5: Tonicity
      7. 5.2.6: Osmoregulation
    3. 5.3: Active Transport
      1. 5.3.0: Electrochemical Gradient
      2. 5.3.1: Primary Active Transport
      3. 5.3.2: Secondary Active Transport
    4. 5.4: Bulk Transport
      1. 5.4.0: Endocytosis
      2. 5.4.1: Exocytosis
  6. 6: Metabolism
    1. 6.1: Energy and Metabolism
      1. 6.1.0: The Role of Energy and Metabolism
      2. 6.1.1: Types of Energy
      3. 6.1.2: Metabolic Pathways
      4. 6.1.3: Metabolism of Carbohydrates
    2. 6.2: Potential, Kinetic, Free, and Activation Energy
      1. 6.2.0: Free Energy
      2. 6.2.1: The First Law of Thermodynamics
      3. 6.2.2: The Second Law of Thermodynamics
      4. 6.2.3: Activation Energy
    3. 6.3: ATP: Adenosine Triphosphate
      1. 6.3.0: ATP: Adenosine Triphosphate
    4. 6.4: Enzymes
      1. 6.4.0: Enzyme Active Site and Substrate Specificity
      2. 6.4.1: Control of Metabolism Through Enzyme Regulation
  7. 7: Cellular Respiration
    1. 7.1: Energy in Living Systems
      1. 7.1.0: Transforming Chemical Energy
      2. 7.1.1: Electrons and Energy
      3. 7.1.2: ATP in Metabolism
    2. 7.2: Glycolysis
      1. 7.2.0: Importance of Glycolysis
      2. 7.2.1: The Energy-Requiring Steps of Glycolysis
      3. 7.2.2: The Energy-Releasing Steps of Glycolysis
      4. 7.2.3: Outcomes of Glycolysis
    3. 7.3: Oxidation of Pyruvate and the Citric Acid Cycle
      1. 7.3.0: Breakdown of Pyruvate
      2. 7.3.1: Acetyl CoA to CO2
      3. 7.3.2: Citric Acid Cycle
    4. 7.4: Oxidative Phosphorylation
      1. 7.4.0: Electron Transport Chain
      2. 7.4.1: Chemiosmosis and Oxidative Phosphorylation
      3. 7.4.2: ATP Yield
    5. 7.5: Metabolism without Oxygen
      1. 7.5.0: Anaerobic Cellular Respiration
    6. 7.6: Connections of Carbohydrate, Protein, and Lipid Metabolic Pathways
      1. 7.6.0: Connecting Other Sugars to Glucose Metabolism
      2. 7.6.1: Connecting Proteins to Glucose Metabolism
      3. 7.6.2: Connecting Lipids to Glucose Metabolism
    7. 7.7: Regulation of Cellular Respiration
      1. 7.7.0: Regulatory Mechanisms for Cellular Respiration
      2. 7.7.1: Control of Catabolic Pathways
  8. 8: Photosynthesis
    1. 8.1: Overview of Photosynthesis
      1. 8.1.0: The Purpose and Process of Photosynthesis
      2. 8.1.1: Main Structures and Summary of Photosynthesis
      3. 8.1.2: The Two Parts of Photosynthesis
    2. 8.2: The Light-Dependent Reactions of Photosynthesis
      1. 8.2.0: Introduction to Light Energy
      2. 8.2.1: Absorption of Light
      3. 8.2.2: Processes of the Light-Dependent Reactions
    3. 8.3: The Light-Independent Reactions of Photosynthesis
      1. 8.3.0: CAM and C4 Photosynthesis
      2. 8.3.1: The Calvin Cycle
      3. 8.3.2: The Carbon Cycle
  9. 9: Cell Communication
    1. 9.1: Signaling Molecules and Cellular Receptors
      1. 9.1.0: Signaling Molecules and Cellular Receptors
      2. 9.1.1: Forms of Signaling
      3. 9.1.2: Types of Receptors
      4. 9.1.3: Signaling Molecules
    2. 9.2: Propagation of the Cellular Signal
      1. 9.2.0: Binding Initiates a Signaling Pathway
      2. 9.2.1: Methods of Intracellular Signaling
    3. 9.3: Response to the Cellular Signal
      1. 9.3.0: Termination of the Signal Cascade
      2. 9.3.1: Cell Signaling and Gene Expression
      3. 9.3.2: Cell Signaling and Cellular Metabolism
      4. 9.3.3: Cell Signaling and Cell Growth
      5. 9.3.4: Cell Signaling and Cell Death
    4. 9.4: Signaling in Single-Celled Organisms
      1. 9.4.0: Signaling in Yeast
      2. 9.4.1: Signaling in Bacteria
  10. 10: Cell Reproduction
    1. 10.1: Cell Division
      1. 10.1.0: The Role of the Cell Cycle
      2. 10.1.1: Genomic DNA and Chromosomes
      3. 10.1.2: Eukaryotic Chromosomal Structure and Compaction
    2. 10.2: The Cell Cycle
      1. 10.2.0: Interphase
      2. 10.2.1: The Mitotic Phase and the G0 Phase
    3. 10.3: Control of the Cell Cycle
      1. 10.3.0: Regulation of the Cell Cycle by External Events
      2. 10.3.1: Regulation of the Cell Cycle at Internal Checkpoints
      3. 10.3.2: Regulator Molecules of the Cell Cycle
    4. 10.4: Cancer and the Cell Cycle
      1. 10.4.0: Proto-oncogenes
      2. 10.4.1: Tumor Suppressor Genes
    5. 10.5: Prokaryotic Cell Division
      1. 10.5.0: Binary Fission
  11. 11: Meiosis and Sexual Reproduction
    1. 11.1: The Process of Meiosis
      1. 11.1.0: Introduction to Meiosis
      2. 11.1.1: Meiosis I
      3. 11.1.2: Meiosis II
      4. 11.1.3: Comparing Meiosis and Mitosis
    2. 11.2: Sexual Reproduction
      1. 11.2.0: Advantages and Disadvantages of Sexual Reproduction
      2. 11.2.1: Life Cycles of Sexually Reproducing Organisms
  12. 12: Mendel's Experiments and Heredity
    1. 12.1: Mendel’s Experiments and the Laws of Probability
      1. 12.1.0: Introduction to Mendelian Inheritance
      2. 12.1.1: Mendel’s Model System
      3. 12.1.2: Mendelian Crosses
      4. 12.1.3: Garden Pea Characteristics Revealed the Basics of Heredity
      5. 12.1.4: Rules of Probability for Mendelian Inheritance
    2. 12.2: Patterns of Inheritance
      1. 12.2.0: Genes as the Unit of Heredity
      2. 12.2.1: Phenotypes and Genotypes
      3. 12.2.2: The Punnett Square Approach for a Monohybrid Cross
      4. 12.2.3: Alternatives to Dominance and Recessiveness
      5. 12.2.4: Sex-Linked Traits
      6. 12.2.5: Lethal Inheritance Patterns
    3. 12.3: Laws of Inheritance
      1. 12.3.0: Mendel's Laws of Heredity
      2. 12.3.1: Mendel's Law of Dominance
      3. 12.3.2: Mendel's Law of Segregation
      4. 12.3.3: Mendel's Law of Independent Assortment
      5. 12.3.4: Genetic Linkage and Violation of the Law of Independent Assortment
      6. 12.3.5: Epistasis
  13. 13: Modern Understandings of Inheritance
    1. 13.1: Chromosomal Theory and Genetic Linkage
      1. 13.1.0: Chromosomal Theory of Inheritance
      2. 13.1.1: Genetic Linkage and Distances
      3. 13.1.2: Identification of Chromosomes and Karyotypes
    2. 13.2: Chromosomal Basis of Inherited Disorders
      1. 13.2.0: Disorders in Chromosome Number
      2. 13.2.1: Chromosomal Structural Rearrangements
      3. 13.2.2: X-Inactivation
  14. 14: DNA Structure and Function
    1. 14.1: Historical Basis of Modern Understanding
      1. 14.1.0: Discovery of DNA
      2. 14.1.1: Modern Applications of DNA
    2. 14.2: DNA Structure and Sequencing
      1. 14.2.0: The Structure and Sequence of DNA
      2. 14.2.1: DNA Sequencing Techniques
    3. 14.3: DNA Replication
      1. 14.3.0: Basics of DNA Replication
      2. 14.3.1: DNA Replication in Prokaryotes
      3. 14.3.2: DNA Replication in Eukaryotes
      4. 14.3.3: Telomere Replication
    4. 14.4: DNA Repair
      1. 14.4.0: DNA Repair
  15. 15: Genes and Proteins
    1. 15.1: The Genetic Code
      1. 15.1.0: The Relationship Between Genes and Proteins
      2. 15.1.1: The Central Dogma: DNA Encodes RNA and RNA Encodes Protein
    2. 15.2: Prokaryotic Transcription
      1. 15.2.0: Transcription in Prokaryotes
      2. 15.2.1: Initiation of Transcription in Prokaryotes
      3. 15.2.2: Elongation and Termination in Prokaryotes
    3. 15.3: Eukaryotic Transcription
      1. 15.3.0: Initiation of Transcription in Eukaryotes
      2. 15.3.1: Elongation and Termination in Eukaryotes
    4. 15.4: RNA Processing in Eukaryotes
      1. 15.4.0: mRNA Processing
      2. 15.4.1: Processing of tRNAs and rRNAs
    5. 15.5: Ribosomes and Protein Synthesis
      1. 15.5.0: The Protein Synthesis Machinery
      2. 15.5.1: The Mechanism of Protein Synthesis
      3. 15.5.2: Protein Folding, Modification, and Targeting
  16. 16: Gene Expression
    1. 16.1: Regulation of Gene Expression
      1. 16.1.0: The Process and Purpose of Gene Expression Regulation
      2. 16.1.1: Prokaryotic versus Eukaryotic Gene Expression
    2. 16.2: Prokaryotic Gene Regulation
      1. 16.2.0: The trp Operon: A Repressor Operon
      2. 16.2.1: Catabolite Activator Protein (CAP): An Activator Regulator
      3. 16.2.2: The lac Operon: An Inducer Operon
    3. 16.3: Eukaryotic Gene Regulation
      1. 16.3.0: The Promoter and the Transcription Machinery
      2. 16.3.1: Transcriptional Enhancers and Repressors
      3. 16.3.2: Epigenetic Control: Regulating Access to Genes within the Chromosome
      4. 16.3.3: RNA Splicing
      5. 16.3.4: The Initiation Complex and Translation Rate
      6. 16.3.5: Regulating Protein Activity and Longevity
    4. 16.4: Regulating Gene Expression in Cell Development
      1. 16.4.0: Gene Expression in Stem Cells
      2. 16.4.1: Cellular Differentiation
      3. 16.4.2: Mechanics of Cellular Differentation
      4. 16.4.3: Establishing Body Axes during Development
      5. 16.4.4: Gene Expression for Spatial Positioning
      6. 16.4.5: Cell Migration in Multicellular Organisms
      7. 16.4.6: Programmed Cell Death
    5. 16.5: Cancer and Gene Regulation
      1. 16.5.0: Altered Gene Expression in Cancer
      2. 16.5.1: Epigenetic Alterations in Cancer
      3. 16.5.2: Cancer and Transcriptional Control
      4. 16.5.3: Cancer and Post-Transcriptional Control
      5. 16.5.4: Cancer and Translational Control
  17. 17: Biotechnology and Genomics
    1. 17.1: Biotechnology
      1. 17.1.0: Biotechnology
      2. 17.1.1: Basic Techniques to Manipulate Genetic Material (DNA and RNA)
      3. 17.1.2: Molecular and Cellular Cloning
      4. 17.1.3: Reproductive Cloning
      5. 17.1.4: Genetic Engineering
      6. 17.1.5: Genetically Modified Organisms (GMOs)
      7. 17.1.6: Biotechnology in Medicine
      8. 17.1.7: Production of Vaccines, Antibiotics, and Hormones
    2. 17.2: Mapping Genomes
      1. 17.2.0: Genetic Maps
      2. 17.2.1: Physical Maps and Integration with Genetic Maps
    3. 17.3: Whole-Genome Sequencing
      1. 17.3.0: Strategies Used in Sequencing Projects
      2. 17.3.1: Use of Whole-Genome Sequences of Model Organisms
      3. 17.3.2: Uses of Genome Sequences
    4. 17.4: Applying Genomics
      1. 17.4.0: Predicting Disease Risk at the Individual Level
      2. 17.4.1: Pharmacogenomics, Toxicogenomics, and Metagenomics
      3. 17.4.2: Genomics and Biofuels
    5. 17.5: Genomics and Proteomics
      1. 17.5.0: Genomics and Proteomics
      2. 17.5.1: Basic Techniques in Protein Analysis
      3. 17.5.2: Cancer Proteomics
  18. 18: Evolution and the Origin of Species
    1. 18.1: Understanding Evolution
      1. 18.1.0: What is Evolution?
      2. 18.1.1: Charles Darwin and Natural Selection
      3. 18.1.2: The Galapagos Finches and Natural Selection
      4. 18.1.3: Processes and Patterns of Evolution
      5. 18.1.4: Evidence of Evolution
      6. 18.1.5: Misconceptions of Evolution
    2. 18.2: Formation of New Species
      1. 18.2.0: The Biological Species Concept
      2. 18.2.1: Reproductive Isolation
      3. 18.2.2: Speciation
      4. 18.2.3: Allopatric Speciation
      5. 18.2.4: Sympatric Speciation
    3. 18.3: Hybrid Zones and Rates of Speciation
      1. 18.3.0: Hybrid Zones
      2. 18.3.1: Varying Rates of Speciation
    4. 18.4: Evolution of Genomes
      1. 18.4.0: Genomic Similiarities between Distant Species
      2. 18.4.1: Genome Evolution
      3. 18.4.2: Whole-Genome Duplication
      4. 18.4.3: Gene Duplications and Divergence
      5. 18.4.4: Noncoding DNA
      6. 18.4.5: Variations in Size and Number of Genes
    5. 18.5: Evidence of Evolution
      1. 18.5.0: The Fossil Record as Evidence for Evolution
      2. 18.5.1: Fossil Formation
      3. 18.5.2: Gaps in the Fossil Record
      4. 18.5.3: Carbon Dating and Estimating Fossil Age
      5. 18.5.4: The Fossil Record and the Evolution of the Modern Horse
      6. 18.5.5: Homologous Structures
      7. 18.5.6: Convergent Evolution
      8. 18.5.7: Vestigial Structures
      9. 18.5.8: Biogeography and the Distribution of Species
  19. 19: The Evolution of Populations
    1. 19.1: Population Evolution
      1. 19.1.0: Defining Population Evolution
      2. 19.1.1: Population Genetics
      3. 19.1.2: Hardy-Weinberg Principle of Equilibrium
    2. 19.2: Population Genetics
      1. 19.2.0: Genetic Variation
      2. 19.2.1: Genetic Drift
      3. 19.2.2: Gene Flow and Mutation
      4. 19.2.3: Nonrandom Mating and Environmental Variance
    3. 19.3: Adaptive Evolution
      1. 19.3.0: Natural Selection and Adaptive Evolution
      2. 19.3.1: Stabilizing, Directional, and Diversifying Selection
      3. 19.3.2: Frequency-Dependent Selection
      4. 19.3.3: Sexual Selection
      5. 19.3.4: No Perfect Organism
  20. 20: Phylogenies and the History of Life
    1. 20.1: Organizing Life on Earth
      1. 20.1.0: Phylogenetic Trees
      2. 20.1.1: Limitations of Phylogenetic Trees
      3. 20.1.2: The Levels of Classification
    2. 20.2: Determining Evolutionary Relationships
      1. 20.2.0: Distinguishing between Similar Traits
      2. 20.2.1: Building Phylogenetic Trees
    3. 20.3: Perspectives on the Phylogenetic Tree
      1. 20.3.0: Limitations to the Classic Model of Phylogenetic Trees
      2. 20.3.1: Horizontal Gene Transfer
      3. 20.3.2: Endosymbiotic Theory and the Evolution of Eukaryotes
      4. 20.3.3: Web, Network, and Ring of Life Models
  21. 21: Viruses
    1. 21.1: Viral Evolution, Morphology, and Classification
      1. 21.1.0: Discovery and Detection of Viruses
      2. 21.1.1: Evolution of Viruses
      3. 21.1.2: Viral Morphology
      4. 21.1.3: Virus Classification
    2. 21.2: Virus Infections and Hosts
      1. 21.2.0: Steps of Virus Infections
      2. 21.2.1: The Lytic and Lysogenic Cycles of Bacteriophages
      3. 21.2.2: Animal Viruses
      4. 21.2.3: Plant Viruses
    3. 21.3: Prevention and Treatment of Viral Infections
      1. 21.3.0: Vaccines and Immunity
      2. 21.3.1: Vaccines and Anti-Viral Drugs for Treatment
    4. 21.4: Prions and Viroids
      1. 21.4.0: Prions and Viroids
  22. 22: Prokaryotes: Bacteria and Archaea
    1. 22.1: Prokaryotic Diversity
      1. 22.1.0: Classification of Prokaryotes
      2. 22.1.1: The Origins of Archaea and Bacteria
      3. 22.1.2: Extremophiles and Biofilms
    2. 22.2: Structure of Prokaryotes
      1. 22.2.0: Basic Structures of Prokaryotic Cells
      2. 22.2.1: Prokaryotic Reproduction
    3. 22.3: Prokaryotic Metabolism
      1. 22.3.0: Energy and Nutrient Requirements for Prokaryotes
      2. 22.3.1: The Role of Prokaryotes in Ecosystems
    4. 22.4: Bacterial Diseases in Humans
      1. 22.4.0: History of Bacterial Diseases
      2. 22.4.1: Biofilms and Disease
      3. 22.4.2: Antibiotics: Are We Facing a Crisis?
      4. 22.4.3: Bacterial Foodborne Diseases
    5. 22.5: Beneficial Prokaryotes
      1. 22.5.0: Symbiosis between Bacteria and Eukaryotes
      2. 22.5.1: Early Biotechnology: Cheese, Bread, Wine, Beer, and Yogurt
      3. 22.5.2: Prokaryotes and Environmental Bioremediation
  23. 23: Protists
    1. 23.1: Eukaryotic Origins
      1. 23.1.0: Early Eukaryotes
      2. 23.1.1: Characteristics of Eukaryotic DNA
      3. 23.1.2: Endosymbiosis and the Evolution of Eukaryotes
      4. 23.1.3: The Evolution of Mitochondria
      5. 23.1.4: The Evolution of Plastids
    2. 23.2: Characteristics of Protists
      1. 23.2.0: Cell Structure, Metabolism, and Motility
      2. 23.2.1: Protist Life Cycles and Habitats
    3. 23.3: Groups of Protists
      1. 23.3.0: Excavata
      2. 23.3.1: Chromalveolata: Alveolates
      3. 23.3.2: Chromalveolata: Stramenopiles
      4. 23.3.3: Rhizaria
      5. 23.3.4: Archaeplastida
      6. 23.3.5: Amoebozoa and Opisthokonta
    4. 23.4: Ecology of Protists
      1. 23.4.0: Protists as Primary Producers, Food Sources, and Symbionts
      2. 23.4.1: Protists as Human Pathogens
      3. 23.4.2: Protists as Plant Pathogens
  24. 24: Fungi
    1. 24.1: Characteristics of Fungi
      1. 24.1.0: Characteristics of Fungi
      2. 24.1.1: Fungi Cell Structure and Function
      3. 24.1.2: Fungi Reproduction
    2. 24.2: Ecology of Fungi
      1. 24.2.0: Fungi Habitat, Decomposition, and Recycling
      2. 24.2.1: Mutualistic Relationships with Fungi and Fungivores
    3. 24.3: Classifications of Fungi
      1. 24.3.0: Chytridiomycota: The Chytrids
      2. 24.3.1: Zygomycota: The Conjugated Fungi
      3. 24.3.2: Ascomycota: The Sac Fungi
      4. 24.3.3: Basidiomycota: The Club Fungi
      5. 24.3.4: Deuteromycota: The Imperfect Fungi
      6. 24.3.5: Glomeromycota
    4. 24.4: Fungal Parasites and Pathogens
      1. 24.4.0: Fungi as Plant, Animal, and Human Pathogens
    5. 24.5: Importance of Fungi in Human Life
      1. 24.5.0: Importance of Fungi in Human Life
  25. 25: Seedless Plants
    1. 25.1: Early Plant Life
      1. 25.1.0: Early Plant Life
      2. 25.1.1: Evolution of Land Plants
      3. 25.1.2: Plant Adaptations to Life on Land
      4. 25.1.3: Sporophytes and Gametophytes in Seedless Plants
      5. 25.1.4: Structural Adaptations for Land in Seedless Plants
      6. 25.1.5: The Major Divisions of Land Plants
    2. 25.2: Green Algae: Precursors of Land Plants
      1. 25.2.0: Streptophytes and Reproduction of Green Algae
      2. 25.2.1: Charales
    3. 25.3: Bryophytes
      1. 25.3.0: Bryophytes
      2. 25.3.1: Liverworts and Hornworts
      3. 25.3.2: Mosses
    4. 25.4: Seedless Vascular Plants
      1. 25.4.0: Seedless Vascular Plants
      2. 25.4.1: Vascular Tissue: Xylem and Phloem
      3. 25.4.2: The Evolution of Roots in Seedless Plants
      4. 25.4.3: Ferns and Other Seedless Vascular Plants
      5. 25.4.4: The Importance of Seedless Vascular Plants
  26. 26: Seed Plants
    1. 26.1: Evolution of Seed Plants
      1. 26.1.0: The Evolution of Seed Plants and Adaptations for Land
      2. 26.1.1: Evolution of Gymnosperms
      3. 26.1.2: Evolution of Angiosperms
    2. 26.2: Gymnosperms
      1. 26.2.0: Characteristics of Gymnosperms
      2. 26.2.1: Life Cycle of a Conifer
      3. 26.2.2: Diversity of Gymnosperms
    3. 26.3: Angiosperms
      1. 26.3.0: Angiosperm Flowers
      2. 26.3.1: Angsiosperm Fruit
      3. 26.3.2: The Life Cycle of an Angiosperm
      4. 26.3.3: Diversity of Angiosperms
    4. 26.4: The Role of Seed Plants
      1. 26.4.0: Herbivory and Pollination
      2. 26.4.1: The Importance of Seed Plants in Human Life
      3. 26.4.2: Biodiversity of Plants
  27. 27: Introduction to Animal Diversity
    1. 27.1: Features of the Animal Kingdom
      1. 27.1.0: Characteristics of the Animal Kingdom
      2. 27.1.1: Complex Tissue Structure
      3. 27.1.2: Animal Reproduction and Development
    2. 27.2: Features Used to Classify Animals
      1. 27.2.0: Animal Characterization Based on Body Symmetry
      2. 27.2.1: Animal Characterization Based on Features of Embryological Development
    3. 27.3: Animal Phylogeny
      1. 27.3.0: Constructing an Animal Phylogenetic Tree
      2. 27.3.1: Molecular Analyses and Modern Phylogenetic Trees
    4. 27.4: The Evolutionary History of the Animal Kingdom
      1. 27.4.0: Pre-Cambrian Animal Life
      2. 27.4.1: The Cambrian Explosion of Animal Life
      3. 27.4.2: Post-Cambrian Evolution and Mass Extinctions
  28. 28: Invertebrates
    1. 28.1: Phylum Porifera
      1. 28.1.0: Phylum Porifera
      2. 28.1.1: Morphology of Sponges
      3. 28.1.2: Physiological Processes in Sponges
    2. 28.2: Phylum Cnidaria
      1. 28.2.0: Phylum Cnidaria
      2. 28.2.1: Class Anthozoa
      3. 28.2.2: Class Scyphozoa
      4. 28.2.3: Class Cubozoa and Class Hydrozoa
    3. 28.3: Superphylum Lophotrochozoa
      1. 28.3.0: Superphylum Lophotrochozoa
      2. 28.3.1: Phylum Platyhelminthes
      3. 28.3.2: Phylum Rotifera
      4. 28.3.3: Phylum Nemertea
      5. 28.3.4: Phylum Mollusca
      6. 28.3.5: Classification of Phylum Mollusca
      7. 28.3.6: Phylum Annelida
    4. 28.4: Superphylum Ecdysozoa
      1. 28.4.0: Superphylum Ecdysozoa
      2. 28.4.1: Phylum Nematoda
      3. 28.4.2: Phylum Arthropoda
      4. 28.4.3: Subphyla of Arthropoda
    5. 28.5: Superphylum Deuterostomia
      1. 28.5.0: Phylum Echinodermata
      2. 28.5.1: Classes of Echinoderms
      3. 28.5.2: Phylum Chordata
  29. 29: Vertebrates
    1. 29.1: Chordates
      1. 29.1.0: Characteristics of Chordata
      2. 29.1.1: Chordates and the Evolution of Vertebrates
      3. 29.1.2: The Evolution of Craniata and Vertebrata
      4. 29.1.3: Characteristics of Vertebrates
    2. 29.2: Fishes
      1. 29.2.0: Agnathans: Jawless Fishes
      2. 29.2.1: Gnathostomes: Jawed Fishes
    3. 29.3: Amphibians
      1. 29.3.0: Characteristics and Evolution of Amphibians
      2. 29.3.1: Modern Amphibians
    4. 29.4: Reptiles
      1. 29.4.0: Characteristics of Amniotes
      2. 29.4.1: Evolution of Amniotes
      3. 29.4.2: Characteristics of Reptiles
      4. 29.4.3: Evolution of Reptiles
      5. 29.4.4: Modern Reptiles
    5. 29.5: Birds
      1. 29.5.0: Characteristics of Birds
      2. 29.5.1: Evolution of Birds
    6. 29.6: Mammals
      1. 29.6.0: Characteristics of Mammals
      2. 29.6.1: Evolution of Mammals
      3. 29.6.2: Living Mammals
    7. 29.7: The Evolution of Primates
      1. 29.7.0: Characteristics and Evolution of Primates
      2. 29.7.1: Early Human Evolution
      3. 29.7.2: Early Hominins
      4. 29.7.3: Genus Homo
  30. 30: Plant Form and Physiology
    1. 30.1: The Plant Body
      1. 30.1.0: Plant Tissues and Organ Systems
    2. 30.2: Stems
      1. 30.2.0: Functions of Stems
      2. 30.2.1: Stem Anatomy
      3. 30.2.2: Primary and Secondary Growth in Stems
      4. 30.2.3: Stem Modifications
    3. 30.3: Roots
      1. 30.3.0: Types of Root Systems and Zones of Growth
      2. 30.3.1: Root Modifications
    4. 30.4: Leaves
      1. 30.4.0: Leaf Structure and Arrangment
      2. 30.4.1: Types of Leaf Forms
      3. 30.4.2: Leaf Structure, Function, and Adaptation
    5. 30.5: Plant Development
      1. 30.5.0: Meristems
      2. 30.5.1: Genetic Control of Flowers
    6. 30.6: Transport of Water and Solutes in Plants
      1. 30.6.0: Water and Solute Potential
      2. 30.6.1: Pressure, Gravity, and Matric Potential
      3. 30.6.2: Movement of Water and Minerals in the Xylem
      4. 30.6.3: Transportation of Photosynthates in the Phloem
    7. 30.7: Plant Sensory Systems and Responses
      1. 30.7.0: Plant Responses to Light
      2. 30.7.1: The Phytochrome System and Red Light Response
      3. 30.7.2: Blue Light Response
      4. 30.7.3: Plant Responses to Gravity
      5. 30.7.4: Auxins, Cytokinins, and Gibberellins
      6. 30.7.5: Abscisic Acid, Ethylene, and Nontraditional Hormones
      7. 30.7.6: Plant Responses to Wind and Touch
    8. 30.8: Plant Defense Mechanisms
      1. 30.8.0: Plant Defenses Against Herbivores
      2. 30.8.1: Plant Defenses Against Pathogens
  31. 31: Soil and Plant Nutrition
    1. 31.1: Nutritional Requirements of Plants
      1. 31.1.0: Plant Nutrition
      2. 31.1.1: The Chemical Composition of Plants
      3. 31.1.2: Essential Nutrients for Plants
    2. 31.2: The Soil
      1. 31.2.0: Soil Composition
      2. 31.2.1: Soil Formation
      3. 31.2.2: Physical Properties of Soil
    3. 31.3: Nutritional Adaptations of Plants
      1. 31.3.0: Nitrogen Fixation: Root and Bacteria Interactions
      2. 31.3.1: Mycorrhizae: The Symbiotic Relationship between Fungi and Roots
      3. 31.3.2: Nutrients from Other Sources
  32. 32: Plant Reproduction
    1. 32.1: Plant Reproductive Development and Structure
      1. 32.1.0: Plant Reproductive Development and Structure
      2. 32.1.1: Sexual Reproduction in Gymnosperms
      3. 32.1.2: Sexual Reproduction in Angiosperms
    2. 32.2: Pollination and Fertilization
      1. 32.2.0: Pollination and Fertilization
      2. 32.2.1: Pollination by Insects
      3. 32.2.2: Pollination by Bats, Birds, Wind, and Water
      4. 32.2.3: Double Fertilization in Plants
      5. 32.2.4: Development of the Seed
      6. 32.2.5: Development of Fruit and Fruit Types
      7. 32.2.6: Fruit and Seed Dispersal
    3. 32.3: Asexual Reproduction
      1. 32.3.0: Asexual Reproduction in Plants
      2. 32.3.1: Natural and Artificial Methods of Asexual Reproduction in Plants
      3. 32.3.2: Plant Life Spans
  33. 33: The Animal Body: Basic Form and Function
    1. 33.1: Animal Form and Function
      1. 33.1.0: Characteristics of the Animal Body
      2. 33.1.1: Body Plans
      3. 33.1.2: Limits on Animal Size and Shape
      4. 33.1.3: Limiting Effects of Diffusion on Size and Development
      5. 33.1.4: Animal Bioenergetics
      6. 33.1.5: Animal Body Planes and Cavities
    2. 33.2: Animal Primary Tissues
      1. 33.2.0: Epithelial Tissues
      2. 33.2.1: Connective Tissues: Loose, Fibrous, and Cartilage
      3. 33.2.2: Connective Tissues: Bone, Adipose, and Blood
      4. 33.2.3: Muscle Tissues and Nervous Tissues
    3. 33.3: Homeostasis
      1. 33.3.0: Homeostatic Process
      2. 33.3.1: Control of Homeostasis
      3. 33.3.2: Homeostasis: Thermoregulation
      4. 33.3.3: Heat Conservation and Dissipation
  34. 34: Animal Nutrition and the Digestive System
    1. 34.1: Digestive Systems
      1. 34.1.0: Digestive Systems
      2. 34.1.1: Herbivores, Omnivores, and Carnivores
      3. 34.1.2: Invertebrate Digestive Systems
      4. 34.1.3: Vertebrate Digestive Systems
      5. 34.1.4: Digestive System: Mouth and Stomach
      6. 34.1.5: Digestive System: Small and Large Intestines
    2. 34.2: Nutrition and Energy Production
      1. 34.2.0: Food Requirements and Essential Nutrients
      2. 34.2.1: Food Energy and ATP
    3. 34.3: Digestive System Processes
      1. 34.3.0: Ingestion
      2. 34.3.1: Digestion and Absorption
      3. 34.3.2: Elimination
    4. 34.4: Digestive System Regulation
      1. 34.4.0: Neural Responses to Food
      2. 34.4.1: Hormonal Responses to Food
  35. 35: The Nervous System
    1. 35.1: Neurons and Glial Cells
      1. 35.1.0: Neurons and Glial Cells
      2. 35.1.1: Neurons
      3. 35.1.2: Glia
    2. 35.2: How Neurons Communicate
      1. 35.2.0: Nerve Impulse Transmission within a Neuron: Resting Potential
      2. 35.2.1: Nerve Impulse Transmission within a Neuron: Action Potential
      3. 35.2.2: Synaptic Transmission
      4. 35.2.3: Signal Summation
      5. 35.2.4: Synaptic Plasticity
    3. 35.3: The Nervous System
      1. 35.3.0: The Nervous System
    4. 35.4: The Central Nervous System
      1. 35.4.0: Brain: Cerebral Cortex and Brain Lobes
      2. 35.4.1: Brain: Midbrain and Brain Stem
      3. 35.4.2: Spinal Cord
    5. 35.5: The Peripheral Nervous System
      1. 35.5.0: Autonomic Nervous System
      2. 35.5.1: Sensory-Somatic Nervous System
    6. 35.6: Nervous System Disorders
      1. 35.6.0: Neurodegenerative Disorders
      2. 35.6.1: Neurodevelopmental Disorders: Autism and ADHD
      3. 35.6.2: Neurodevelopmental Disorders: Mental Illnesses
      4. 35.6.3: Other Neurological Disorders
  36. 36: Sensory Systems
    1. 36.1: Sensory Processes
      1. 36.1.0: Reception
      2. 36.1.1: Transduction and Perception
    2. 36.2: Somatosensation
      1. 36.2.0: Somatosensory Receptors
      2. 36.2.1: Integration of Signals from Mechanoreceptors
      3. 36.2.2: Thermoreception
    3. 36.3: Taste and Smell
      1. 36.3.0: Tastes and Odors
      2. 36.3.1: Reception and Transduction
    4. 36.4: Hearing and Vestibular Sensation
      1. 36.4.0: Sound
      2. 36.4.1: Reception of Sound
      3. 36.4.2: Transduction of Sound
      4. 36.4.3: The Vestibular System
      5. 36.4.4: Balance and Determining Equilibrium
    5. 36.5: Vision
      1. 36.5.0: Light
      2. 36.5.1: Anatomy of the Eye
      3. 36.5.2: Transduction of Light
      4. 36.5.3: Visual Processing
  37. 37: The Endocrine System
    1. 37.1: Types of Hormones
      1. 37.1.0: Hormone Functions
      2. 37.1.1: Lipid-Derived, Amino Acid-Derived, and Peptide Hormones
    2. 37.2: How Hormones Work
      1. 37.2.0: How Hormones Work
      2. 37.2.1: Intracellular Hormone Receptors
      3. 37.2.2: Plasma Membrane Hormone Receptors
    3. 37.3: Regulation of Body Processes
      1. 37.3.0: Hormonal Regulation of the Excretory System
      2. 37.3.1: Hormonal Regulation of the Reproductive System
      3. 37.3.2: Hormonal Regulation of Metabolism
      4. 37.3.3: Hormonal Control of Blood Calcium Levels
      5. 37.3.4: Hormonal Regulation of Growth
      6. 37.3.5: Hormonal Regulation of Stress
    4. 37.4: Regulation of Hormone Production
      1. 37.4.0: Humoral, Hormonal, and Neural Stimuli
    5. 37.5: Endocrine Glands
      1. 37.5.0: Hypothalamic-Pituitary Axis
      2. 37.5.1: Thyroid Gland
      3. 37.5.2: Parathyroid Glands
      4. 37.5.3: Adrenal Glands
      5. 37.5.4: Pancreas
      6. 37.5.5: Pineal Gland and Gonads
      7. 37.5.6: Organs with Secondary Endocrine Functions
  38. 38: The Musculoskeletal System
    1. 38.1: Types of Skeletal Systems
      1. 38.1.0: Functions of the Musculoskeletal System
      2. 38.1.1: Types of Skeletal Systems
      3. 38.1.2: Human Axial Skeleton
      4. 38.1.3: Human Appendicular Skeleton
    2. 38.2: Bone
      1. 38.2.0: Bone
      2. 38.2.1: Cell Types in Bones
      3. 38.2.2: Bone Development
      4. 38.2.3: Growth of Bone
      5. 38.2.4: Bone Remodeling and Repair
    3. 38.3: Joints and Skeletal Movement
      1. 38.3.0: Classification of Joints on the Basis of Structure and Function
      2. 38.3.1: Movement at Synovial Joints
      3. 38.3.2: Types of Synovial Joints
      4. 38.3.3: Bone and Joint Disorders
    4. 38.4: Muscle Contraction and Locomotion
      1. 38.4.0: Structure and Function of the Muscular System
      2. 38.4.1: Skeletal Muscle Fibers
      3. 38.4.2: Sliding Filament Model of Contraction
      4. 38.4.3: ATP and Muscle Contraction
      5. 38.4.4: Regulatory Proteins
      6. 38.4.5: Excitation–Contraction Coupling
      7. 38.4.6: Control of Muscle Tension
  39. 39: The Respiratory System
    1. 39.1: Systems of Gas Exchange
      1. 39.1.0: The Respiratory System and Direct Diffusion
      2. 39.1.1: Skin, Gills, and Tracheal Systems
      3. 39.1.2: Amphibian and Bird Respiratory Systems
      4. 39.1.3: Mammalian Systems and Protective Mechanisms
    2. 39.2: Gas Exchange across Respiratory Surfaces
      1. 39.2.0: Gas Pressure and Respiration
      2. 39.2.1: Basic Principles of Gas Exchange
      3. 39.2.2: Lung Volumes and Capacities
      4. 39.2.3: Gas Exchange across the Alveoli
    3. 39.3: Breathing
      1. 39.3.0: The Mechanics of Human Breathing
      2. 39.3.1: Types of Breathing
      3. 39.3.2: The Work of Breathing
      4. 39.3.3: Dead Space: V/Q Mismatch
    4. 39.4: Transport of Gases in Human Bodily Fluids
      1. 39.4.0: Transport of Oxygen in the Blood
      2. 39.4.1: Transport of Carbon Dioxide in the Blood
  40. 40: The Circulatory System
    1. 40.1: Overview of the Circulatory System
      1. 40.1.0: The Role of the Circulatory System
      2. 40.1.1: Open and Closed Circulatory Systems
      3. 40.1.2: Types of Circulatory Systems in Animals
    2. 40.2: Components of the Blood
      1. 40.2.0: The Role of Blood in the Body
      2. 40.2.1: Red Blood Cells
      3. 40.2.2: White Blood Cells
      4. 40.2.3: Platelets and Coagulation Factors
      5. 40.2.4: Plasma and Serum
    3. 40.3: Mammalian Heart and Blood Vessels
      1. 40.3.0: Structures of the Heart
      2. 40.3.1: Arteries, Veins, and Capillaries
      3. 40.3.2: The Cardiac Cycle
    4. 40.4: Blood Flow and Blood Pressure Regulation
      1. 40.4.0: Blood Flow Through the Body
      2. 40.4.1: Blood Pressure
  41. 41: Osmotic Regulation and the Excretory System
    1. 41.1: Osmoregulation and Osmotic Balance
      1. 41.1.0: Introduction to Osmoregulation
      2. 41.1.1: Transport of Electrolytes across Cell Membranes
      3. 41.1.2: Concept of Osmolality and Milliequivalent
      4. 41.1.3: Osmoregulators and Osmoconformers
    2. 41.2: Nitrogenous Wastes
      1. 41.2.0: Nitrogenous Waste in Terrestrial Animals: The Urea Cycle
      2. 41.2.1: Nitrogenous Waste in Birds and Reptiles: Uric Acid
    3. 41.3: Excretion Systems
      1. 41.3.0: Contractile Vacuoles in Microorganisms
      2. 41.3.1: Flame Cells of Planaria and Nephridia of Worms
      3. 41.3.2: Malpighian Tubules of Insects
    4. 41.4: Human Osmoregulatory and Excretory Systems
      1. 41.4.0: Kidney Structure
      2. 41.4.1: Nephron: The Functional Unit of the Kidney
      3. 41.4.2: Kidney Function and Physiology
    5. 41.5: Hormonal Control of Osmoregulatory Functions
      1. 41.5.0: Epinephrine and Norepinephrine
      2. 41.5.1: Other Hormonal Controls for Osmoregulation
  42. 42: The Immune System
    1. 42.1: Innate Immune Response
      1. 42.1.0: Innate Immune Response
      2. 42.1.1: Physical and Chemical Barriers
      3. 42.1.2: Pathogen Recognition
      4. 42.1.3: Natural Killer Cells
      5. 42.1.4: The Complement System
    2. 42.2: Adaptive Immune Response
      1. 42.2.0: Antigen-presenting Cells: B and T cells
      2. 42.2.1: Humoral Immune Response
      3. 42.2.2: Cell-Mediated Immunity
      4. 42.2.3: Cytotoxic T Lymphocytes and Mucosal Surfaces
      5. 42.2.4: Immunological Memory
      6. 42.2.5: Regulating Immune Tolerance
    3. 42.3: Antibodies
      1. 42.3.0: Antibody Structure
      2. 42.3.1: Antibody Functions
    4. 42.4: Disruptions in the Immune System
      1. 42.4.0: Immunodeficiency
      2. 42.4.1: Hypersensitivities
  43. 43: Animal Reproduction and Development
    1. 43.1: Reproduction Methods
      1. 43.1.0: Methods of Reproducing
      2. 43.1.1: Types of Sexual and Asexual Reproduction
      3. 43.1.2: Sex Determination
    2. 43.2: Fertilization
      1. 43.2.0: External and Internal Fertilization
      2. 43.2.1: The Evolution of Reproduction
    3. 43.3: Human Reproductive Anatomy and Gametogenesis
      1. 43.3.0: Male Reproductive Anatomy
      2. 43.3.1: Female Reproductive Anatomy
      3. 43.3.2: Gametogenesis (Spermatogenesis and Oogenesis)
    4. 43.4: Hormonal Control of Human Reproduction
      1. 43.4.0: Male Hormones
      2. 43.4.1: Female Hormones
    5. 43.5: Fertilization and Early Embryonic Development
      1. 43.5.0: Fertilization
      2. 43.5.1: Cleavage, the Blastula Stage, and Gastrulation
    6. 43.6: Organogenesis and Vertebrate Formation
      1. 43.6.0: Organogenesis
      2. 43.6.1: Vertebrate Axis Formation
    7. 43.7: Human Pregnancy and Birth
      1. 43.7.0: Human Gestation
      2. 43.7.1: Labor and Birth
      3. 43.7.2: Contraception and Birth Control
      4. 43.7.3: Infertility
  44. 44: Ecology and the Biosphere
    1. 44.1: The Scope of Ecology
      1. 44.1.0: Introduction to Ecology
      2. 44.1.1: Organismal Ecology and Population Ecology
      3. 44.1.2: Community Ecology and Ecosystem Ecology
    2. 44.2: Biogeography
      1. 44.2.0: Biogeography
      2. 44.2.1: Energy Sources
      3. 44.2.2: Temperature and Water
      4. 44.2.3: Inorganic Nutrients and Other Factors
      5. 44.2.4: Abiotic Factors Influencing Plant Growth
    3. 44.3: Terrestrial Biomes
      1. 44.3.0: What constitutes a biome?
      2. 44.3.1: Tropical Wet Forest and Savannas
      3. 44.3.2: Subtropical Deserts and Chaparral
      4. 44.3.3: Temperate Grasslands
      5. 44.3.4: Temperate Forests
      6. 44.3.5: Boreal Forests and Arctic Tundra
    4. 44.4: Aquatic Biomes
      1. 44.4.0: Abiotic Factors Influencing Aquatic Biomes
      2. 44.4.1: Marine Biomes
      3. 44.4.2: Estuaries: Where the Ocean Meets Fresh Water
      4. 44.4.3: Freshwater Biomes
    5. 44.5: Climate and the Effects of Global Climate Change
      1. 44.5.0: Climate and Weather
      2. 44.5.1: Causes of Global Climate Change
      3. 44.5.2: Evidence of Global Climate Change
      4. 44.5.3: Past and Present Effects of Climate Change
  45. 45: Population and Community Ecology
    1. 45.1: Population Demography
      1. 45.1.0: Population Demography
      2. 45.1.1: Population Size and Density
      3. 45.1.2: Species Distribution
      4. 45.1.3: The Study of Population Dynamics
    2. 45.2: Environmental Limits to Population Growth
      1. 45.2.0: Exponential Population Growth
      2. 45.2.1: Logistic Population Growth
      3. 45.2.2: Density-Dependent and Density-Independent Population Regulation
    3. 45.3: Life History Patterns
      1. 45.3.0: Life History Patterns and Energy Budgets
      2. 45.3.1: Theories of Life History
    4. 45.4: Human Population Growth
      1. 45.4.0: Human Population Growth
      2. 45.4.1: Overcoming Density-Dependent Regulation
      3. 45.4.2: Age Structure, Population Growth, and Economic Development
    5. 45.5: Community Ecology
      1. 45.5.0: The Role of Species within Communities
      2. 45.5.1: Predation, Herbivory, and the Competitive Exclusion Principle
      3. 45.5.2: Symbiosis
      4. 45.5.3: Ecological Succession
    6. 45.6: Innate Animal Behavior
      1. 45.6.0: Introduction to Animal Behavior
      2. 45.6.1: Movement and Migration
      3. 45.6.2: Animal Communication and Living in Groups
      4. 45.6.3: Altruism and Populations
      5. 45.6.4: Mating Systems and Sexual Selection
    7. 45.7: Learned Animal Behavior
      1. 45.7.0: Simple Learned Behaviors
      2. 45.7.1: Conditioned Behavior
      3. 45.7.2: Cognitive Learning and Sociobiology
  46. 46: Ecosystems
    1. 46.1: Ecology of Ecosystems
      1. 46.1.0: Ecosystem Dynamics
      2. 46.1.1: Food Chains and Food Webs
      3. 46.1.2: Studying Ecosystem Dynamics
      4. 46.1.3: Modeling Ecosystem Dynamics
    2. 46.2: Energy Flow through Ecosystems
      1. 46.2.0: Strategies for Acquiring Energy
      2. 46.2.1: Productivity within Trophic Levels
      3. 46.2.2: Transfer of Energy between Trophic Levels
      4. 46.2.3: Ecological Pyramids
      5. 46.2.4: Biological Magnification
    3. 46.3: Biogeochemical Cycles
      1. 46.3.0: Biogeochemical Cycles
      2. 46.3.1: The Water (Hydrologic) Cycle
      3. 46.3.2: The Carbon Cycle
      4. 46.3.3: The Nitrogen Cycle
      5. 46.3.4: The Phosphorus Cycle
      6. 46.3.5: The Sulfur Cycle
  47. 47: Conservation Biology and Biodiversity
    1. 47.1: The Biodiversity Crisis
      1. 47.1.0: Loss of Biodiversity
      2. 47.1.1: Types of Biodiversity
      3. 47.1.2: Biodiversity Change through Geological Time
      4. 47.1.3: The Pleistocene Extinction
      5. 47.1.4: Present-Time Extinctions
    2. 47.2: The Importance of Biodiversity to Human Life
      1. 47.2.0: Human Health and Biodiversity
      2. 47.2.1: Agricultural Diversity
      3. 47.2.2: Managing Fisheries
    3. 47.3: Threats to Biodiversity
      1. 47.3.0: Habitat Loss and Sustainability
      2. 47.3.1: Overharvesting
      3. 47.3.2: Exotic Species
      4. 47.3.3: Climate Change and Biodiversity
    4. 47.4: Preserving Biodiversity
      1. 47.4.0: Measuring Biodiversity
      2. 47.4.1: Changing Human Behavior in Response to Biodiversity Loss
      3. 47.4.2: Ecological Restoration

15.5: Ribosomes and Protein Synthesis

15.5.1: The Protein Synthesis Machinery

Protein synthesis, or translation of mRNA into protein, occurs with the help of ribosomes, tRNAs, and aminoacyl tRNA synthetases.

Learning Objective

Explain the role played by ribosomes, tRNA, and aminoacyl tRNA synthetases in protein synthesis

Key Points

  • Ribosomes, macromolecular structures composed of rRNA and polypeptide chains, are formed of two subunits (in bacteria and archaea, 30S and 50S; in eukaryotes, 40S and 60S), that bring together mRNA and tRNAs to catalyze protein synthesis.
  • Fully assembled ribosomes have three tRNA binding sites: an A site for incoming aminoacyl-tRNAs, a P site for peptidyl-tRNAs, and an E site where empty tRNAs exit.
  • tRNAs (transfer ribonucleic acids), which serve to deliver the appropriate amino acid to the growing peptide chain, consist of a modified RNA chain with the appropriate amino acid covalently attached.
  • tRNAs have a loop of unbasepaired nucleotides at one end of the molecule that contains three nucleotides that act as the anticodon that basepairs to the mRNA codon.
  • Aminoacyl tRNA synthetases are enzymes that load the individual amino acids onto the tRNAs.

Key Term

ribosome

protein/mRNA complexes found in all cells that are involved in the production of proteins by translating messenger RNA

The Protein Synthesis Machinery

In addition to the mRNA template, many molecules and macromolecules contribute to the process of translation. The composition of each component may vary across species. For instance, ribosomes may consist of different numbers of rRNAs and polypeptides depending on the organism. However, the general structures and functions of the protein synthesis machinery are comparable from bacteria to archaea to human cells. Translation requires the input of an mRNA template, ribosomes, tRNAs, and various enzymatic factors.

Ribosomes

A ribosome is a complex macromolecule composed of structural and catalytic rRNAs, and many distinct polypeptides. In eukaryotes, the synthesis and assembly of rRNAs occurs in the nucleolus.

The ribosome in action

The ribosome in action

Structure and role of ribosomes during translation

Ribosomes exist in the cytoplasm in prokaryotes and in the cytoplasm and on rough endoplasmic reticulum membranes in eukaryotes. Mitochondria and chloroplasts also have their own ribosomes, and these look more similar to prokaryotic ribosomes (and have similar drug sensitivities) than the cytoplasmic ribosomes. Ribosomes dissociate into large and small subunits when they are not synthesizing proteins and reassociate during the initiation of translation.E. coli have a 30S small subunit and a 50S large subunit, for a total of 70S when assembled (recall that Svedberg units are not additive). Mammalian ribosomes have a small 40S subunit and a large 60S subunit, for a total of 80S. The small subunit is responsible for binding the mRNA template, whereas the large subunit sequentially binds tRNAs.

In bacteria, archaea, and eukaryotes, the intact ribosome has three binding sites that accomodate tRNAs: The A site, the P site, and the E site. Incoming aminoacy-tRNAs (a tRNA with an amino acid covalently attached is called an aminoacyl-tRNA) enter the ribosome at the A site. The peptidyl-tRNA carrying the growing polypeptide chain is held in the P site. The E site holds empty tRNAs just before they exit the ribosome.

Ribosome structure

Ribosome structure

The large ribosomal subunit sits atop the small ribosomal subunit and the mRNA is threaded through a groove near the interface of the two subunits. The intact ribosome has three tRNA binding sites: the A site for incoming aminoacyl-tRNAs; the P site for the peptidyl-tRNA carrying the growing polypeptide chain; and the E site where empty tRNAs exit (not shown in this figure but immediately adjacent to the P site.)

Each mRNA molecule is simultaneously translated by many ribosomes, all reading the mRNA from 5' to 3' and synthesizing the polypeptide from the N terminus to the C terminus. The complete mRNA/poly-ribosome structure is called a polysome.

tRNAs in eukaryotes

The tRNA molecules are transcribed by RNA polymerase III. Depending on the species, 40 to 60 types of tRNAs exist in the cytoplasm. Specific tRNAs bind to codons on the mRNA template and add the corresponding amino acid to the polypeptide chain. (More accurately, the growing polypeptide chain is added to each new amino acid bound in by a tRNA.)

The transfer RNAs (tRNAs) are structural RNA molecules. In eukaryotes, tRNA mole are transcribed from tRNA genes by RNA polymerase III. Depending on the species, 40 to 60 types of tRNAs exist in the cytoplasm. Serving as adaptors, specific tRNAs bind to sequences on the mRNA template and add the corresponding amino acid to the polypeptide chain. (More accurately, the growing polypeptide chain is added to each new amino acid brought in by a tRNA.) Therefore, tRNAs are the molecules that actually "translate" the language of RNA into the language of proteins.

Of the 64 possible mRNA codons (triplet combinations of A, U, G, and C) three specify the termination of protein synthesis and 61 specify the addition of amino acids to the polypeptide chain. Of the three termination codons, one (UGA) can also be used to encode the 21st amino acid, selenocysteine, but only if the mRNA contains a specific sequence of nucleotides known as a SECIS sequence. Of the 61 non-termination codons, one codon (AUG) also encodes the initiation of translation.

Each tRNA polynucleotide chain folds up so that some internal sections basepair with other internal sections. If just diagrammed in two dimensions, the regions where basepairing occurs are called stems, and the regions where no basepairs form are called loops, and the entire pattern of stems and loops that forms for a tRNA is called the "cloverleaf" structure. All tRNAs fold into very similar cloverleaf structures of four major stems and three major loops.

The two-dimensional cloverleaf structure of a typical tRNA.

The two-dimensional cloverleaf structure of a typical tRNA.

All tRNAs, regardless of the species they come from or the amino acid they carry, self-basepair to produce a cloverleaf structure of four main stems and three main loops. The amino acid carried by the tRNA is covalently attached to the nucleotide at the 3' end of the tRNA, known as the tRNA's acceptor arm. The opposite end of the folded tRNA has the anticodon loop where the tRNA will basepair to the mRNA codon.

If viewed as a three-dimensional structure, all the basepaired regions of the tRNA are helical, and the tRNA folds into a L-shaped structure.

The three dimensional shape taken by tRNAs.

The three dimensional shape taken by tRNAs.

If viewed as a three-dimensional structure, all tRNAs are partially helical molecules that are vaguely L-shaped. The anticodon-containing loop is at one end of the molecule (in grey here) and the amino acid acceptor arm is at the other end of the molecule (in yellow here) past the bend of the "L".

Each tRNA has a sequence of three nucleotides located in a loop at one end of the molecule that can basepair with an mRNA codon. This is called the tRNA's anticodon. Each different tRNA has a different anticodon. When the tRNA anticodon basepairs with one of the mRNA codons, the tRNA will add an amino acid to a growing polypeptide chain or terminate translation, according to the genetic code. For instance, if the sequence CUA occurred on a mRNA template in the proper reading frame, it would bind a tRNA with an anticodon expressing the complementary sequence, GAU. The tRNA with this anticodon would be linked to the amino acid leucine.

Aminoacyl tRNA Synthetases

The process of pre-tRNA synthesis by RNA polymerase III only creates the RNA portion of the adaptor molecule. The corresponding amino acid must be added later, once the tRNA is processed and exported to the cytoplasm. Through the process of tRNA "charging," each tRNA molecule is linked to its correct amino acid by a group of enzymes called aminoacyl tRNA synthetases. When an amino acid is covalently linked to a tRNA, the resulting complex is known as an aminoacyl-tRNA. At least one type of aminoacyl tRNA synthetase exists for each of the 21 amino acids; the exact number of aminoacyl tRNA synthetases varies by species. These enzymes first bind and hydrolyze ATP to catalyze the formation of a covalent bond between an amino acid and adenosine monophosphate (AMP); a pyrophosphate molecule is expelled in this reaction. This is called "activating" the amino acid. The same enzyme then catalyzes the attachment of the activated amino acid to the tRNA and the simultaneous release of AMP. After the correct amino acid covalently attached to the tRNA, it is released by the enzyme. The tRNA is said to be charged with its cognate amino acid. (the amino acid specified by its anticodon is a tRNA's cognate amino acid.)

15.5.2: The Mechanism of Protein Synthesis

Protein synthesis involves building a peptide chain using tRNAs to add amino acids and mRNA as a blueprint for the specific sequence.

Learning Objective

Describe the process of translation

Key Points

  • Protein synthesis, or translation, begins with a process known as pre-initiation, when the small ribosmal subunit, the mRNA template, initiator factors, and a special initiator tRNA, come together.
  • During translocation and elongation, the ribosome moves one codon 3' down the mRNA, brings in a charged tRNA to the A site, transfers the growing polypeptide chain from the P-site tRNA to the carboxyl group of the A-site amino acid, and ejects the uncharged tRNA at the E site.
  • When a stop or nonsense codon (UAA, UAG, or UGA) is reached on the mRNA, the ribosome terminates translation.

Key Term

translation

a process occurring in the ribosome in which a strand of messenger RNA (mRNA) guides assembly of a sequence of amino acids to make a protein

The Mechanism of Protein Synthesis

As with mRNA synthesis, protein synthesis can be divided into three phases: initiation, elongation, and termination.

Initiation of Translation

Protein synthesis begins with the formation of a pre-initiation complex. In E. coli, this complex involves the small 30S ribosome, the mRNA template, three initiation factors (IFs; IF-1, IF-2, and IF-3), and a special initiator tRNA, called fMet-tRNA. The initiator tRNA basepairs to the start codon AUG (or rarely, GUG) and is covalently linked to a formylated methionine called fMet. Methionine is one of the 21 amino acids used in protein synthesis; formylated methionine is a methione to which a formyl group (a one-carbon aldehyde) has been covalently attached at the amino nitrogen. Formylated methionine is inserted by fMet-tRNA at the beginning of every polypeptide chain synthesized by E. coli, and is usually clipped off after translation is complete. When an in-frame AUG is encountered during translation elongation, a non-formylated methionine is inserted by a regular Met-tRNA. In E. coli mRNA, a sequence upstream of the first AUG codon, called the Shine-Dalgarno sequence (AGGAGG), interacts with the rRNA molecules that compose the ribosome. This interaction anchors the 30S ribosomal subunit at the correct location on the mRNA template.

In eukaryotes, a pre-initiation complex forms when an initiation factor called eIF2 (eukaryotic initiation factor 2) binds GTP, and the GTP-eIF2 recruits the eukaryotic initiator tRNA to the 40s small ribosomal subunit. The initiator tRNA, called Met-tRNAi, carries unmodified methionine in eukaryotes, not fMet, but it is distinct from other cellular Met-tRNAs in that it can bind eIFs and it can bind at the ribosome P site. The eukaryotic pre-initiation complex then recognizes the 7-methylguanosine cap at the 5' end of a mRNA. Several other eIFs, specifically eIF1, eIF3, and eIF4, act as cap-binding proteins and assist the recruitment of the pre-initiation complex to the 5' cap. Poly (A)-Binding Protein (PAB) binds both the poly (A) tail of the mRNA and the complex of proteins at the cap and also assists in the process. Once at the cap, the pre-initiation complex tracks along the mRNA in the 5' to 3' direction, searching for the AUG start codon. Many, but not all, eukaryotic mRNAs are translated from the first AUG sequence. The nucleotides around the AUG indicate whether it is the correct start codon.

Once the appropriate AUG is identified, eIF2 hydrolyzes GTP to GDP and powers the delivery of the tRNAi-Met to the start codon, where the tRNAi anticodon basepairs to the AUG codon. After this, eIF2-GDP is released from the complex, and eIF5-GTP binds. The 60S ribosomal subunit is recruited to the pre-initiation complex by eIF5-GTP, which hydrolyzes its GTP to GDP to power the assembly of the full ribosome at the translation start site with the Met-tRNAi positioned in the ribosome P site. The remaining eIFs dissociate from the ribosome and translation is ready to begins.

In archaea, translation initiation is similar to that seen in eukaryotes, except that the initiation factors involved are called aIFs (archaeal inititiaion factors), not eIFs.

Translation initiation in eukaryotes.

Translation initiation in eukaryotes.

In eukaryotes, a preinitiation complex forms made of the small 40S subunit, the initiator Met-tRNAi, and eIF2-GTP. This preinitiation complex binds to the 5'-m7G cap of the mRNA with the help of other eIFS and PAB, which binds the poly(A) tail of the mRNA, and loops the tail to the cap. Once at the cap, the preinitiation complex slides along the mRNA until it encounters the initiator AUG codon. There, GTP is hydrolyzed by eIF2 and the Met-tRNAi is loaded onto the AUG. Next, eIF5-GTP recruits the 60S large ribosomal subunit to the 40S subunit at the AUG and hydrolyzes GTP. This allows the large ribosomal subunit to assemble on top of the small subunit, generating the intact 80S ribosome, and places the Met-tRNAi in the P site of the intact ribosome . The ribosome A site is positioned over the second codon in the mRNA reading frame, and translation elongation can begin.

Translation Elongation

The basics of elongation are the same in prokaryotes and eukaryotes. The intact ribosome has three compartments: the A site binds incoming aminoacyl tRNAs; the P site binds tRNAs carrying the growing polypeptide chain; the E site releases dissociated tRNAs so that they can be recharged with amino acids. The initiator tRNA, rMet-tRNA in E. coli and Met-tRNAi in eukaryotes and archaea, binds directly to the P site. This creates an initiation complex with a free A site ready to accept the aminoacyl-tRNA corresponding to the first codon after the AUG.

The aminoacyl-tRNA with an anticodon complementary to the A site codon lands in the A site. A peptide bond is formed between the amino group of the A site amino acid and the carboxyl group of the most-recently attached amino acid in the growing polypeptide chain attached to the P-site tRNA.The formation of the peptide bond is catalyzed by peptidyl transferase, an RNA-based enzyme that is integrated into the large ribosomal subunit. The energy for the peptide bond formation is derived from GTP hydrolysis, which is catalyzed by a separate elongation factor.

Catalyzing the formation of a peptide bond removes the bond holding the growing polypeptide chain to the P-site tRNA. The growing polypeptide chain is transferred to the amino end of the incoming amino acid, and the A-site tRNA temporarily holds the growing polypeptide chain, while the P-site tRNA is now empty or uncharged.

The ribosome moves three nucleotides down the mRNA. The tRNAs are basepaired to a codon on the mRNA, so as the ribosome moves over the mRNA, the tRNAs stay in place while the ribosome moves and each tRNA is moved into the next tRNA binding site. The E site moves over the former P-site tRNA, now empty or uncharged, the P site moves over the former A-site tRNA, now carrying the growing polypeptide chain, and the A site moves over a new codon. In the E site, the uncharged tRNA detaches from its anticodon and is expelled . A new aminoacyl-tRNA with an anticodon complementary to the new A-site codon enters the ribosome at the A site and the elongation process repeats itself. The energy for each step of the ribosome is donated by an elongation factor that hydrolyzes GTP.

Translation elongation in eukaryotes.

Translation elongation in eukaryotes.

During translation elongation, the incoming aminoacyl-tRNA enters the ribosome A site, where it binds if the tRNA anticodon is complementary to the A site mRNA codon. The elongation factor eEF1 assists in loading the aminoacyl-tRNA, powering the process through the hydrolysis of GTP. The growing polypeptide chain is attached to the tRNA in the ribosome P site. The ribosome's peptidyl transferase catalyses the transfer of the growing polypeptide chain from the P site tRNA to the amino group of the A site amino acid. This creates a peptide bond between the C terminus of the growing polypeptide chain and the A site amino acid. After the peptide bond is created, the growing polypeptide chain is attached to the A site tRNA, and the tRNA in the P site is empty. The ribosome translocates once codon on the mRNA. The elongation factor eEF2 assists in the translocation, powering the process through the hydrolysis of GTP. During translocation, the two tRNAs remain basepaired to their mRNA codons, so the ribosome moves over them, putting the empty tRNA in the E site (where it will be expelled from the ribosome) and the tRNA with the growing polypeptide chain in the P site. The A site moves over an empty codon, and the process repeats itself until a stop codon is reached.

Translation termination

Termination of translation occurs when the ribosome moves over a stop codon (UAA, UAG, or UGA). There are no tRNAs with anticodons complementary to stop codons, so no tRNAs enter the A site. Instead, in both prokaryotes and eukaryotes, a protein called a release factor enters the A site. The release factors cause the ribosome peptidyl transferase to add a water molecule to the carboxyl end of the most recently added amino acid in the growing polypeptide chain attached to the P-site tRNA. This causes the polypeptide chain to detach from its tRNA, and the newly-made polypeptide is released. The small and large ribosomal subunits dissociate from the mRNA and from each other; they are recruited almost immediately into another translation initiation complex. After many ribosomes have completed translation, the mRNA is degraded so the nucleotides can be reused in another transcription reaction.

15.5.3: Protein Folding, Modification, and Targeting

In order to function, proteins must fold into the correct three-dimensional shape, and be targeted to the correct part of the cell.

Learning Objective

Discuss how post-translational events affect the proper function of a protein

Key Points

  • Protein folding is a process in which a linear chain of amino acids attains a defined three-dimensional structure, but there is a possibility of forming misfolded or denatured proteins, which are often inactive.
  • Proteins must also be located in the correct part of the cell in order to function correctly; therefore, a signal sequence is often attached to direct the protein to its proper location, which is removed after it attains its location.
  • Protein misfolding is the cause of numerous diseases, such as mad cow disease, Creutzfeldt-Jakob disease, and cystic fibrosis.

Key Terms

chaperone

a protein that assists the non-covalent folding/unfolding of other proteins

prion

a self-propagating misfolded conformer of a protein that is responsible for a number of diseases that affect the brain and other neural tissue

Protein Folding

After being translated from mRNA, all proteins start out on a ribosome as a linear sequence of amino acids. This linear sequence must "fold" during and after the synthesis so that the protein can acquire what is known as its native conformation . The native conformation of a protein is a stable three-dimensional structure that strongly determines a protein's biological function. When a protein loses its biological function as a result of a loss of three-dimensional structure, we say that the protein has undergone denaturation. Proteins can be denatured not only by heat, but also by extremes of pH; these two conditions affect the weak interactions and the hydrogen bonds that are responsible for a protein's three-dimensional structure. Even if a protein is properly specified by its corresponding mRNA, it could take on a completely dysfunctional shape if abnormal temperature or pH conditions prevent it from folding correctly. The denatured state of the protein does not equate with the unfolding of the protein and randomization of conformation. Actually, denatured proteins exist in a set of partially-folded states that are currently poorly understood. Many proteins fold spontaneously, but some proteins require helper molecules, called chaperones, to prevent them from aggregating during the complicated process of folding.

Protein folding

Protein folding

A protein starts as a linear sequence of amino acids, then folds into a 3-dimensional shape imbued with all the functional properties required inside the cell.

Protein Modification and Targeting

During and after translation, individual amino acids may be chemically modified and signal sequences may be appended to the protein. A signal sequence is a short tail of amino acids that directs a protein to a specific cellular compartment. These sequences at the amino end or the carboxyl end of the protein can be thought of as the protein's "train ticket" to its ultimate destination. Other cellular factors recognize each signal sequence and help transport the protein from the cytoplasm to its correct compartment. For instance, a specific sequence at the amino terminus will direct a protein to the mitochondria or chloroplasts (in plants). Once the protein reaches its cellular destination, the signal sequence is usually clipped off.

Misfolding

It is very important for proteins to achieve their native conformation since failure to do so may lead to serious problems in the accomplishment of its biological function. Defects in protein folding may be the molecular cause of a range of human genetic disorders. For example, cystic fibrosis is caused by defects in a membrane-bound protein called cystic fibrosis transmembrane conductance regulator (CFTR). This protein serves as a channel for chloride ions. The most common cystic fibrosis-causing mutation is the deletion of a Phe residue at position 508 in CFTR, which causes improper folding of the protein. Many of the disease-related mutations in collagen also cause defective folding.

A misfolded protein, known as prion, appears to be the agent of a number of rare degenerative brain diseases in mammals, like the mad cow disease. Related diseases include kuru and Creutzfeldt-Jakob. The diseases are sometimes referred to as spongiform encephalopathies, so named because the brain becomes riddled with holes. Prion, the misfolded protein, is a normal constituent of brain tissue in all mammals, but its function is not yet known. Prions cannot reproduce independently and not considered living microoganisms. A complete understanding of prion diseases awaits new information about how prion protein affects brain function, as well as more detailed structural information about the protein. Therefore, improved understanding of protein folding may lead to new therapies for cystic fibrosis, Creutzfeldt-Jakob, and many other diseases.

Attributions

  • The Protein Synthesis Machinery
    • "Boundless." http://www.boundless.com/. Boundless Learning CC BY-SA 3.0.
    • "ribosome." http://en.wiktionary.org/wiki/ribosome. Wiktionary CC BY-SA 3.0.
    • "OpenStax College, Biology. October 16, 2013." http://cnx.org/content/m44529/latest/?collection=col11448/latest. OpenStax CNX CC BY 3.0.
    • "Ribosome." http://en.wikipedia.org/wiki/Ribosome. Wikipedia CC BY-SA.
    • "Transfer RNA." http://commons.wikimedia.org/wiki/File:TRNA-Phe_yeast_en.svg. Wikipedia CC BY-SA 3.0.
    • "Transfer RNA." http://commons.wikimedia.org/wiki/File:TRNA-Phe_yeast_en.svg. Wikepedia CC BY-SA 3.0.
    • "Translation (biology)." http://en.wikipedia.org/wiki/Translation_(biology)%23mediaviewer/File:Ribosome_mRNA_translation_en.svg. Wikepedia Public domain.
  • The Mechanism of Protein Synthesis
    • "Boundless." http://www.boundless.com/. Boundless Learning CC BY-SA 3.0.
    • "translation." http://en.wiktionary.org/wiki/translation. Wiktionary CC BY-SA 3.0.
    • "OpenStax College, Biology. October 16, 2013." http://cnx.org/content/m44529/latest/?collection=col11448/latest. OpenStax CNX CC BY 3.0.
    • "Original figure by Ross Whitwam. Licensed CC BY-SA 4.0." Ross Whitwam CC BY-SA 3.0.
    • "Original figure by Ross Whitwam. Licensed CC BY-SA 4.0." Ross Whitwam CC BY-SA 3.0.
  • Protein Folding, Modification, and Targeting
    • "Boundless." http://www.boundless.com/. Boundless Learning CC BY-SA 3.0.
    • "chaperone." http://en.wiktionary.org/wiki/chaperone. Wiktionary CC BY-SA 3.0.
    • "Lydia Kavraki, Protein Folding. November 4, 2013." http://cnx.org/content/m11467/latest/. OpenStax CNX CC BY 3.0.
    • "prion." http://en.wiktionary.org/wiki/prion. Wiktionary CC BY-SA 3.0.
    • "OpenStax College, Biology. October 16, 2013." http://cnx.org/content/m44529/latest/?collection=col11448/latest. OpenStax CNX CC BY 3.0.
    • "Protein folding." http://en.wikipedia.org/wiki/File:Protein_folding.png. Wikipedia Public domain.

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