Higher Level Biology for the IB Diploma Programme

Höfundur Alan Damon; Randy McGonegal; William Ward

Útgefandi Pearson International Content

Snið Page Fidelity

Print ISBN 9781292427744

Útgáfa 3

Höfundarréttur 2023

3.690 kr.

Description

Efnisyfirlit

  • Contents
  • Syllabus roadmap
  • Authors’ introduction to the third edition
  • Theme A
  • A Unity and diversity – Molecules
  • A1.1: Water
  • A1.1.1 – The medium of life
  • A1.1.2 – The structure and polarity of water molecules
  • A1.1.3 – Cohesion of water molecules
  • A1.1.4 – Adhesion between water and other polar substances
  • A1.1.5 – The solvent properties of water
  • A1.1.6 – The physical properties of water
  • A1.1.7 – The origin of water on Earth
  • A1.1.8 – The search for extraterrestrial life
  • A1.2 Nucleic acids
  • A1.2.1 – DNA is the universal genetic material
  • A1.2.2 – The structure of nucleotides
  • A1.2.3 – Sugar to phosphate “backbone” of DNA and RNA
  • A1.2.4 – Nitrogenous bases within nucleic acids
  • A1.2.5 – The structure of RNA
  • A1.2.6 – The structure of DNA
  • A1.2.7 – Distinguishing between DNA and RNA
  • A1.2.8 – The importance of complementary base pairing
  • A1.2.9 – Storage of genetic information
  • A1.2.10 – Genetic uniqueness
  • A1.2.11 – Directionality of RNA and DNA strands
  • A1.2.12 – Purine-to-pyrimidine bonding
  • A1.2.13 – Efficient packaging of DNA molecules
  • A1.2.14 – The Hershey–Chase experiment
  • A1.2.15 – Chargaff’s rule
  • A Unity and diversity – Cells
  • A2.1: Origins of cells
  • A2.1.1 – The formation of carbon compounds
  • A2.1.2 – Functions of life
  • A2.1.3 – Evolution of the cell
  • A2.1.4 – Inorganic to carbon compounds
  • A2.1.5 – The formation of vesicles
  • A2.1.6 – RNA as the first genetic material
  • A2.1.7 – Evidence for a last universal common ancestor
  • A2.1.8 – Dating the first living cells and LUCA
  • A2.1.9 – Hydrothermal vents and the evolution of the LUCA
  • A2.2: Cell structure
  • A2.2.1 – Cells and the functions of life
  • A2.2.2 – Cells and the microscope
  • A2.2.3 – Advanced microscopy
  • A2.2.4 – Structures common to all cells
  • A2.2.5 – The prokaryote cell
  • A2.2.6 – The eukaryote cell
  • A2.2.7 – Unicellular organisms
  • A2.2.8 – Different types of eukaryotic cells
  • A2.2.9 – Atypical eukaryotes
  • A2.2.10 and A2.2.11 – Electron micrograph skills
  • A2.2.12 – The origin of eukaryotic cells
  • A2.2.13 and A2.2.14 – Cell specialization and multicellularity
  • A2.3: Viruses
  • A2.3.1 – Characteristics of viruses
  • A2.3.2 – Structural diversity in viruses
  • A2.3.3 and A2.3.4 – The life cycle of viruses
  • A2.3.5 – The origin of viruses
  • A2.3.6 – Rapidly evolving viruses
  • A Unity and diversity – Organisms
  • A3.1: Diversity of organisms
  • A3.1.1 – Variation between organisms
  • A3.1.2 – Species as groups of organisms
  • A3.1.3 – The binomial naming system
  • A3.1.4 – Biological species
  • A3.1.5 – Distinguishing between populations and species
  • A3.1.6 – Diversity in chromosome numbers
  • A3.1.7 – Karyotypes
  • A3.1.8 – Unity and diversity of genomes
  • A3.1.9 – Eukaryote genomes
  • A3.1.10 – Genome sizes
  • A3.1.11 – Whole genome sequencing
  • A3.1.12 – Difficulties with the biological species concept
  • A3.1.13 – Chromosome number as a shared trait
  • A3.1.14 – Dichotomous keys
  • A3.1.15 – DNA barcoding
  • A3.2: Classification and cladistics
  • A3.2.1 – The classification of organisms
  • A3.2.2 – Difficulties in classifying organisms
  • A3.2.3 – Classification using evolutionary relationships
  • A3.2.4 – Clades display common ancestries and shared characteristics
  • A3.2.5 – The evolutionary clock
  • A3.2.6 – Constructing cladograms
  • A3.2.7 – Using cladograms
  • A3.2.8 – Cladistics and reclassification
  • A3.2.9 – Three domains of life, not two
  • A Unity and diversity – Ecosystems
  • A4.1: Evolution and speciation
  • A4.1.1 – Evolution
  • A4.1.2 – Biochemical evidence for evolution
  • A4.1.3 – Selective breeding
  • A4.1.4 – Homologous and analogous structures
  • A4.1.5 – Convergent evolution
  • A4.1.6 – Speciation
  • A4.1.7 – Reproductive isolation and differential selection
  • A4.1.8 – Allopatric and sympatric speciation
  • A4.1.9 – Adaptive radiation
  • A4.1.10 – Barriers to hybridization, and hybrid sterility
  • A4.1.11 – Abrupt speciation in plants
  • A4.2: Conservation of biodiversity
  • A4.2.1 – Biodiversity exists in many forms
  • A4.2.2 – Has biodiversity changed over time?
  • A4.2.3 – Human activities and the rate of species extinction
  • A4.2.4 – Human activities and ecosystem loss
  • A4.2.5 – A biodiversity crisis
  • A4.2.6 – Causes of the biodiversity crisis
  • A4.2.7 – Conservation of biodiversity
  • A4.2.8 – The EDGE of Existence programme
  • Theme B
  • B Form and function – Molecules
  • B1.1: Carbohydrates and lipids
  • B1.1.1 – The variety of compounds containing carbon
  • B1.1.2 and B1.1.3 – Condensation and hydrolysis
  • B1.1.4 – Monosaccharides
  • B1.1.5 – Polysaccharides and energy storage
  • B1.1.6 – Cellulose as a structural polysaccharide
  • B1.1.7 – Conjugated carbon molecules
  • B1.1.8 – Lipid solubility
  • B1.1.9 – Triglycerides and phospholipids
  • B1.1.10 – Properties of fatty acids
  • B1.1.11 – Adipose tissue
  • B1.1.12 – Phospholipid bilayers
  • B1.1.13 – Steroid hormones
  • B1.2: Proteins
  • B1.2.1 – The common structure of amino acids
  • B1.2.2 – Condensation reactions bond amino acids together
  • B1.2.3 – Essential amino acids
  • B1.2.4 – The vast variety of polypeptides
  • B1.2.5 – The effect of pH and temperature
  • B1.2.6 – R-groups provide diversity
  • B1.2.7 – Primary structure of a protein
  • B1.2.8 – Secondary structure of a protein
  • B1.2.9 – Tertiary structure of a protein
  • B1.2.10 – Polar and non-polar amino acids
  • B1.2.11 – Quaternary structure of proteins
  • B1.2.12 – Protein shape and its function
  • B Form and function – Cells
  • B2.1: Membranes and membrane transport
  • B2.1.1 and B2.1.2 – Membrane structure
  • B2.1.3 – Diffusion across cellular membranes
  • B2.1.4 – Membrane proteins
  • B2.1.5 and B2.1.6 – Membrane transport
  • B2.1.7 – Active transport and pump proteins
  • B2.1.8 – Membrane permeability
  • B2.1.9 – Glycoproteins and glycolipids
  • B2.1.10 – The fluid mosaic model
  • B2.1.11 – Fatty acids and membrane fluidity
  • B2.1.12 – Cholesterol and membrane fluidity
  • B2.1.13 – Bulk transport and membrane fluidity
  • B2.1.14 – Gated ion channels and cellular transport
  • B2.1.15 – The sodium−potassium pump
  • B2.1.16 – Indirect active transport
  • B2.1.17 – Cell adhesion
  • B2.2: Organelles and compartmentalization
  • B2.2.1 – Cell compartmentalization
  • B2.2.2 – The nucleus and cytoplasm
  • B2.2.3 – Compartmentalization of the cytoplasm
  • B2.2.4 – The mitochondrion
  • B2.2.5 – The chloroplast
  • B2.2.6 – The double membrane of the nucleus
  • B2.2.7 – The ribosome
  • B2.2.8 – The Golgi apparatus
  • B2.2.9 – Cellular vesicles
  • B2.3: Cell specialization
  • B2.3.1 – Cell reproduction and organism development
  • B2.3.2 – Stem cells
  • B2.3.3 – Stem cell niches
  • B2.3.4 – Types of stem cell
  • B2.3.5 – Cell size and specialization
  • B2.3.6 – Constraints on cell size
  • B2.3.7 – Surface area-to-volume adaptations
  • B2.3.8 – Lung alveoli
  • B2.3.9 – Muscle fibres
  • B2.3.10 – Sperm and egg cells
  • B Form and function – Organisms
  • B3.1: Gas exchange
  • B3.1.1 – The exchange of gases between organisms and their environment
  • B3.1.2 – Gas exchange surfaces
  • B3.1.3 – Concentration gradients at exchange surfaces in animals
  • B3.1.4 – Gas exchange in mammalian lungs
  • B3.1.5 – Lung ventilation
  • B3.1.6 – Lung volume
  • B3.1.7 – Gas exchange in leaves
  • B3.1.8 – Leaf tissue distribution
  • B3.1.9 – Transpiration
  • B3.1.10 – Stomata
  • B3.1.11 – Haemoglobin and oxygen transport
  • B.3.1.12 – The Bohr shift
  • B3.1.13 – Oxygen dissociation curves
  • B3.2: Transport
  • B3.2.1 – Capillaries and chemical exchange
  • B3.2.2 – Arteries and veins
  • B3.2.3 – Adaptations of arteries
  • B3.2.4 – Measuring the pulse rate
  • B3.2.5 – Adaptations of veins
  • B3.2.6 – Occlusion of coronary arteries
  • B3.2.7 – Water transport from roots to leaves
  • B3.2.8 – Adaptations of xylem vessels
  • B3.2.9 – Tissues in a dicotyledonous stem
  • B3.2.10 – Tissues in a dicotyledonous root
  • B3.2.11 – Capillaries and tissue fluid
  • B3.2.12 – Exchange between cells and tissue fluid
  • B3.2.13 – Lymph ducts
  • B3.2.14 – Single and double circulation
  • B3.2.15 – The mammalian heart
  • B3.2.16 – The cardiac cycle
  • B3.2.17 – Xylem root pressure
  • B3.2.18 – Phloem translocation of sap
  • B3.3: Muscle and motility
  • B3.3.1 – Adaptations for movement
  • B3.3.2 – The sliding filament theory
  • B3.3.3 – Antagonistic muscle pairs and titin
  • B3.3.4 – Motor units
  • B3.3.5 – Skeletons as levers and anchor points
  • B3.3.6 – Synovial joints
  • B3.3.7 – Range of motion
  • B3.3.8 – Antagonistic muscle action
  • B3.3.9 – The need for locomotion
  • B3.3.10 – Swimming adaptations
  • B Form and function – Ecosystems
  • B4.1: Adaptation to environment
  • B4.1.1 – What is a habitat?
  • B4.1.2 – Adaptation to the abiotic environment
  • B4.1.3 – Abiotic variables
  • B4.1.4 – Limiting factors
  • B4.1.5 – Coral reef formation
  • B4.1.6 – Terrestrial biomes
  • B4.1.7 – Biomes, ecosystems and communities
  • B4.1.8 – Hot deserts and tropical rainforests
  • B4.2: Ecological niches
  • B4.2.1 – Species and ecosystems
  • B4.2.2 – Obligate anaerobes, facultative anaerobes and obligate aerobes
  • B4.2.3 – Photosynthesis
  • B4.2.4 – Holozoic nutrition
  • B4.2.5 – Mixotrophic nutrition
  • B4.2.6 – Saprotrophic nutrition
  • B4.2.7 – Diversity of nutrition in archaea
  • B4.2.8 – The relationship between dentition and diet
  • B4.2.9 – Adaptations of herbivores and plants
  • B4.2.10 – Adaptations of predators and prey
  • B4.2.11 – Harvesting light
  • B4.2.12 – Ecological niches
  • B4.2.13 – Competitive exclusion
  • Theme C
  • C Interaction and interdependence – Molecules
  • C1.1: Enzymes and metabolism
  • C1.1.1 – Enzymes as catalysts
  • C1.1.2 – Metabolism
  • C1.1.3 – Anabolism and catabolism
  • C1.1.4 – Globular proteins and active sites
  • C1.1.5 and C1.1.10 – Enzyme activation
  • C1.1.6 – Molecular motion
  • C1.1.7 – Mechanism of enzyme action
  • C1.1.8 – Factors affecting enzyme-catalysed reactions
  • C1.1.9 – Measuring enzyme-catalysed reactions
  • C1.1.11 – Intracellular and extracellular reactions
  • C1.1.12 – Metabolic efficiency
  • C1.1.13 – Metabolic pathways
  • C1.1.14 – Non-competitive inhibition
  • C1.1.15 – Competitive inhibition
  • C1.1.16 – Feedback inhibition
  • C1.1.17 – Mechanism-based inhibition
  • C1.2: Cell respiration
  • C1.2.1 – ATP structure and function
  • C1.2.2 – Life processes within cells require ATP
  • C1.2.3 – ATP and ADP
  • C1.2.4 and C1.2.5 – ATP and cell respiration
  • C1.2.6 – The rate of cell respiration
  • C1.2.7 – The role of NAD in cellular respiration
  • C1.2.8 – Glycolysis, ATP and NAD
  • C1.2.9 – The fate of pyruvate
  • C1.2.10 – Anaerobic cell respiration in yeast
  • C1.2.11 – The link reaction
  • C1.2.12 – Oxidation and decarboxylation in the Krebs cycle
  • C1.2.13 – Reduced NAD
  • C1.2.14 and C1.2.15 – The electron transport chain and chemiosmosis
  • C1.2.16 – The role of oxygen
  • C1.2.17 – Respiratory substrates
  • C1.3: Photosynthesis
  • C1.3.1 – Light energy and life processes
  • C1.3.2 and C1.3.3 – The equation for photosynthesis
  • C1.3.4 – Photosynthetic pigments and light absorption
  • C1.3.5 and C1.3.6 – Absorption and action spectra
  • C1.3.7 – Measuring the rate of photosynthesis
  • C1.3.8 – Carbon dioxide levels and future rates of photosynthesis
  • C1.3.9 – Light-dependent reactions and photosystems
  • C1.3.10 – Advantages of the structured array
  • C1.3.11 – Oxygen as a waste product
  • C1.3.12 and C1.3.13 – Photophosphorylation
  • C1.3.14 – The role of thylakoids
  • C1.3.15, C1.3.16 and C1.3.17 – Light independentreactions and the Calvin cycle
  • C1.3.18 – Synthesis of other carbohydrates and amino acids
  • C1.3.19 – Overview of photosynthesis
  • C Interaction and interdependence – Cells
  • C2.1: Chemical signalling
  • C2.1.1 – The requirements for cell signalling
  • C2.1.2 – Quorum sensing in bacteria
  • C2.1.3 – Functional categories of animal signalling chemicals
  • C2.1.4 – The diversity of signalling chemicals
  • C2.1.5 – The range of effects of signalling molecules
  • C2.1.6 and C2.1.7 – Differences between transmembrane and intracellular receptors
  • C2.1.8 – Acetylcholine and changes to membrane potential
  • C2.1.9 and C2.1.10 – G protein-coupled receptors
  • C2.1.11 – Tyrosine kinase activity
  • C2.1.12 – Intracellular receptors and gene expression
  • C2.1.13 – Effects of oestradiol and progesterone on target cells
  • C2.1.14 – Regulation of cell signalling pathways
  • C2.2 – Neural signalling
  • C2.2.1 – The role of neurons
  • C2.2.2 and C2.2.3 – Generation and transmission of an impulse along a neuron
  • C2.2.4 – The speed of nerve impulses
  • C2.2.5 and C2.2.6 – Synapses,neurotransmitters, and their actions
  • C2.2.7 – Acetylcholine and the generation of a postsynaptic potential
  • C2.2.8, C2.2.9 and C2.2.10 – Neuron depolarization and repolarization
  • C2.2.11 – Saltatory conduction in myelinated axons
  • C2.2.12 – The effect of exogenous chemicals
  • C2.2.13 – Neurotransmitters and postsynaptic potentials
  • C2.2.14 – Summation of inhibitory and excitatory effects
  • C2.2.15 – Perception of pain
  • C2.2.16 – Consciousness as an emergent property
  • C Interaction and interdependence – Organisms
  • C3.1: Integration of body systems
  • C3.1.1 – Coordinating systems
  • C3.1.2 – Hierarchy of body subsystems
  • C3.1.3 – Integration of organs in animals
  • C3.1.4 – The brain and information processing
  • C3.1.5 – The spinal cord and unconscious processes
  • C3.1.6 – Sensory neurons and conveying information
  • C3.1.7 – Motor neurons and muscle stimulation
  • C3.1.8 – Nerve fibres
  • C3.1.9 – Pain reflex arcs
  • C3.1.10 – The cerebellum and skeletal muscle coordination
  • C3.1.11 – Melatonin secretion and sleep patterns
  • C3.1.12 – Epinephrine and vigorous activity
  • C3.1.13 – The hypothalamus, pituitary gland and endocrine system
  • C3.1.14 – Feedback control of heart rate
  • C3.1.15 – Feedback control of ventilation rate
  • C3.1.16 – Control of peristalsis in the alimentary canal
  • C3.1.17 and C3.1.18 – Tropic responses
  • C3.1.19 – Plant hormones
  • C3.1.20 – Auxin efflux carriers
  • C3.1.21 – Plant cell elongation
  • C3.1.22 – Integration of root and shoot growth
  • C3.1.23 – Feedback control of fruit ripening
  • C3.2: Defence against disease
  • C3.2.1 – Infectious diseases are caused by pathogens
  • C3.2.2 – Skin and mucous membranes as the first line of defence
  • C3.2.3 – Blood clotting minimizes blood loss and infection
  • C3.2.4 – A two-layered immune system: innate and adaptive
  • C3.2.5 – The role of phagocytes
  • C3.2.6 – The role of lymphocytes
  • C3.2.7 – Antigens trigger antibody production
  • C3.2.8 – The role of helper T-lymphocytes
  • C3.2.9 – Activation of a B-lymphocyte results in cloning
  • C3.2.10 – The role of memory cells
  • C3.2.11 – HIV transmission
  • C3.2.12 – The result of HIV infection
  • C3.2.13 – Antibiotics against bacterial infections
  • C3.2.14 – Pathogenic resistance to antibiotics
  • C3.2.15 – Zoonotic diseases
  • C3.2.16 – Vaccines and immunity
  • C3.2.17 – The role of herd immunity
  • C3.2.18 – Evaluating COVID-19 data
  • C Interaction and interdependence – Ecosystems
  • C4.1: Populations and communities
  • C4.1.1 – Populations
  • C4.1.2 – Estimating population size
  • C4.1.3 – Sampling sessile organisms
  • C4.1.4 – Sampling motile organisms
  • C4.1.5 – Carrying capacity
  • C4.1.6 – Negative feedback
  • C4.1.7 – Population growth
  • C4.1.8 – Modelling population growth
  • C4.1.9 – Communities
  • C4.1.10 – Intraspecific relationships
  • C4.1.11 – Interspecific relationships
  • C4.1.12 – Mutualism
  • C4.1.13 – Endemic and invasive species
  • C4.1.14 – Interspecific competition
  • C4.1.15 – The chi-squared test
  • C4.1.16 – Predator–prey relationships
  • C4.1.17 – Control of populations
  • C4.1.18 – Allelopathy and antibiotic secretion
  • C4.2: Transfers of energy and matter
  • C4.2.1 – Ecosystems are open systems
  • C4.2.2 – Sunlight sustains most ecosystems
  • C4.2.3 – The flow of energy
  • C4.2.4 – Food chains and food webs
  • C4.2.5 – Decomposers
  • C4.2.6 – Autotrophs
  • C4.2.7 – Energy sources
  • C4.2.8 – Heterotrophs
  • C4.2.9 – The release of energy by cell respiration
  • C4.2.10 – Trophic levels
  • C4.2.11 – Energy pyramids
  • C4.2.12 – Energy loss between trophic levels
  • C4.2.13 – Heat loss from cell respiration
  • C4.2.14 – The number of trophic levels
  • C4.2.15 – Primary production
  • C4.2.16 – Secondary production
  • C4.2.17 – The carbon cycle
  • C4.2.18 – Carbon sinks and sources
  • C4.2.19 – The release of carbon dioxide during combustion
  • C4.2.20 – The Keeling Curve
  • C4.2.21 – The dependence on atmospheric oxygen and carbon dioxide
  • C4.2.22 – The recycling of chemical elements
  • Theme D
  • D Continuity and change – Molecules
  • D1.1: DNA replication
  • D1.1.1 – The role of DNA replication
  • D1.1.2 and D1.1.3 – Semi-conservative replication and complementary base pairing
  • D1.1.4 – Amplifying and separating DNA
  • D1.1.5 – Applications of amplifying and separating DNA
  • D1.1.6 – DNA polymerases
  • D1.1.7 – Leading and lagging strands
  • D1.1.8 – Functions of specifi c enzymes and molecules
  • D1.1.9 – Removing mismatched nucleotides
  • D1.2: Protein synthesis
  • D1.2.1 – The synthesis of RNA
  • D1.2.2 – Hydrogen bonding and complementary base pairing
  • D1.2.3 – DNA templates
  • D1.2.4 – The expression of genes
  • D1.2.5 – The synthesis of polypeptides
  • D1.2.6 – RNA and ribosomes
  • D1.2.7 – RNA complementary base pairing
  • D1.2.8 – The genetic code
  • D1.2.9 – mRNA codons
  • D1.2.10 – Producing a polypeptide chain
  • D1.2.11 – Changing the protein structure
  • D1.2.12 – Directionality
  • D1.2.13 – Initiating transcription
  • D1.2.14 – Non-coding sequences
  • D1.2.15 – Post-transcriptional modification
  • D1.2.16 – Alternative splicing of exons
  • D1.2.17 – Initiating translation
  • D1.2.18 – Modifying polypeptides
  • D1.2.19 – Recycling amino acids
  • D1.3: Mutation and gene editing
  • D1.3.1 – Gene mutations
  • D1.3.2 – Base substitutions
  • D1.3.3 – Insertions and deletions
  • D1.3.4 – Mutagens and replication errors
  • D1.3.5 – Location of mutations
  • D1.3.6 – Mutations in germ cells and somatic cells
  • D1.3.7 – Genetic variation
  • D1.3.8 – Gene knockout
  • D1.3.9 – CRISPR-Cas9 gene editing
  • D1.3.10 – Conserved and highly conserved sequences
  • D Continuity and change – Cells
  • D2.1: Cell and nuclear division
  • D2.1.1 – Generating new cells
  • D2.1.2 – Cytokinesis
  • D2.1.3 – Cytoplasm division
  • D2.1.4 – Nuclear division
  • D2.1.5 – DNA replication
  • D2.1.6 – DNA condensation and chromosome movement
  • D2.1.7 – Mitosis
  • D2.1.8 – Identifying the phases of mitosis
  • D2.1.9 – Meiosis
  • D2.1.10 – Non-disjunction
  • D2.1.11 – Genetic diversity
  • D2.1.12 – Cell proliferation
  • D2.1.13 – The cell cycle
  • D2.1.14 – Interphase
  • D2.1.15 – Cyclins
  • D2.1.16 – The effect of mutations
  • D2.1.17 – Tumour growth
  • D2.2: Gene expression
  • D2.2.1 – Phenotype
  • D2.2.2 – Regulation of transcription
  • D2.2.3 – Degradation of mRNA to regulate translation
  • D2.2.4 – Epigenesis
  • D2.2.5 – Genome, transcriptome and proteome
  • D2.2.6 – Methylation
  • D2.2.7 – Epigenetic inheritance
  • D2.2.8 – Environmental effects
  • D2.2.9 – Removal of epigenetic tags
  • D2.2.10 – Monozygotic twins
  • D2.2.11 – External factors
  • D2.3: Water potential
  • D2.3.1 – Water as a solvent
  • D2.3.2 – Water movement in relation to solute concentration
  • D2.3.3 and D2.3.4 – Hypotonic and hypertonic solutions and osmosis
  • D2.3.5 – Water movement without cell walls
  • D2.3.6 – Water movement with cell walls
  • D2.3.7 – Isotonic solutions
  • D2.3.8, D2.3.9 and D2.3.10 – Water movement through plants
  • D2.3.11 – Water potential in plant tissue
  • D Continuity and change – Organisms
  • D3.1: Reproduction
  • D3.1.1 – Sexual and asexual reproduction
  • D3.1.2 – The role of meiosis and gametes
  • D3.1.3 – Male and female gametes
  • D3.1.4 – Male and female reproductive systems
  • D3.1.5 – Hormonal control of the menstrual cycle
  • D3.1.6 – The process of fertilization
  • D3.1.7 – In vitro fertilization
  • D3.1.8 – Sexual reproduction in plants
  • D3.1.9 – Insect pollination
  • D3.1.10 – Cross-pollination in plants
  • D3.1.11 – Self-incompatibility mechanisms
  • D3.1.12 – The role of seeds
  • D3.1.13 – Developmental changes during puberty
  • D3.1.14 – The production of gametes
  • D3.1.15 – Preventing polyspermy
  • D3.1.16 – Embryo development
  • D3.1.17 – Pregnancy testing
  • D3.1.18 – The role of the placenta
  • D3.1.19 – Pregnancy and childbirth
  • D3.1.20 – Hormone replacement therapy
  • D3.2: Inheritance
  • D3.2.1 – Haploid gametes and diploid zygotes
  • D3.2.2 – Genetic crosses in flowering plants
  • D3.2.3 – Combinations of alleles
  • D3.2.4 – Phenotype
  • D3.2.5 – Dominant and recessive alleles
  • D3.2.6 – Phenotypic plasticity
  • D3.2.7 – Recessive genetic conditions
  • D3.2.8 – Single-nucleotide polymorphisms and multiple alleles
  • D3.2.9 – ABO blood groups
  • D3.2.10 – Intermediate and dual phenotypes
  • D3.2.11 – Sex determination
  • D3.2.12 – Haemophilia
  • D3.2.13 – Pedigree charts
  • D3.2.14 – Continuous variation
  • D3.2.15 – Box-and-whisker plots
  • D3.2.16 – Segregation and independent assortment
  • D3.2.17 – Predicting genotypic and phenotypic ratios
  • D3.2.18 – Gene loci and polypeptide products
  • D3.2.19 – Gene linkage
  • D3.2.20 – Recombinants
  • D3.2.21 – Chi-squared tests
  • D3.3 Homeostasis
  • D3.3.1 – Maintaining the body’s internal environment
  • D3.3.2 – Negative feedback mechanisms
  • D3.3.3 – The role of hormones
  • D3.3.4 – Type 1 and type 2 diabetes
  • D3.3.5 and D3.3.6 – Body temperature control
  • D3.3.7 – The role of the kidneys
  • D3.3.8 – The glomerulus, Bowman’s capsule and proximal convoluted tubule
  • D3.3.9 – The loop of Henle
  • D3.3.10 – Osmoregulation
  • D3.3.11 – Variable blood supply dependent on activity
  • D Continuity and change – Ecosystems
  • D4.1: Natural selection
  • D4.1.1 – Evolutionary change
  • D4.1.2 – Sources of variation
  • D4.1.3 – Overproduction and competition
  • D4.1.4 – Selection pressure
  • D4.1.5 – Intraspecific competition
  • D4.1.6 – Heritable traits
  • D4.1.7 – Sexual selection
  • D4.1.8 – Modelling selection pressures
  • D4.1.9 – Gene pools
  • D4.1.10 – Geographically isolated populations
  • D4.1.11 – Changes in allele frequency
  • D4.1.12 – Reproductive isolation of populations
  • D4.1.13 – The Hardy–Weinberg equation
  • D 4.1.14 – Genetic equilibrium
  • D4.1.15 – Artificial selection
  • D4.2: Stability and change
  • D4.2.1 – Sustainability of natural ecosystems
  • D4.2.2 – Requirements for sustainability
  • D4.2.3 – Tipping points
  • D4.2.4 – Mesocosms
  • D4.2.5 – Keystone species
  • D4.2.6 – Sustainable harvesting of natural resources
  • D4.2.7 – Sustainability of agriculture
  • D4.2.8 – Eutrophication
  • D4.2.9 – Biomagnification
  • D4.2.10 – Microplastic and macroplastic pollution
  • D4.2.11 – Rewilding
  • D4.2.12 – Ecological succession
  • D4.2.13 – Primary succession
  • D4.2.14 – Cyclical succession
  • D4.2.15 – Climax communities
  • D4.3: Climate change
  • D4.3.1 – Human activity and climate change
  • D4.3.2 – Global warming
  • D4.3.3 – Tipping points
  • D4.3.4 – Polar habitat change
  • D4.3.5 – Ocean current change
  • D4.3.6 – Range shifts
  • D4.3.7 – Ecosystem collapse
  • D4.3.8 – Carbon sequestration
  • D4.3.9 – Phenology
  • D4.3.10 – Disruption of phenological events
  • D4.3.11 – Insect life cycles
  • D4.3.12 – Evolution and climate change
  • Theory of Knowledge in biology
  • Internal Assessment
  • Skills in the study of biology
  • Extended Essay
  • Index
  • Back Cover
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