CAPE Biology Unit 1 Comprehensive Study Notes

  • Biochemistry is the study of biological molecules and their roles in organisms. These molecules are considered the building blocks of life, constantly being assembled and disassembled through metabolism.
  • Metabolism is the collective term for all chemical reactions in an organism, divided into two categories:     - Anabolism: Reactions that build larger biological molecules from smaller ones (anabolic reactions).     - Catabolism: Reactions that break down large biological molecules into smaller ones (catabolic reactions).
  • All major biological compounds are based on the element carbon, which forms strong covalent bonds with itself and other atoms, producing both single and double bonds.
  • Inorganic compounds in the air include oxygen, carbon dioxide, nitrogen, and hydrogen. Complex compounds of carbon are categorized as organic compounds.
  • Key Chemical Terms:     - Chemical element: A pure substance consisting of one type of atom.     - Atom: The smallest component of an element containing neutrons and protons in a nucleus, surrounded by electrons.     - Isotope: Atoms of the same element with different numbers of neutrons.     - Molecule: The smallest particle of a substance retaining physical/chemical properties, composed of two or more atoms.     - Ion: An atom or molecule that has gained or lost electrons, acquiring a positive or negative charge.     - Ionic bond: A chemical bond between two ions with opposite charges.     - Covalent bond: A chemical bond involving the sharing of an electron pair between atoms.
  • Biological macromolecules are often polymers made of repeating sub-units called monomers:     - Carbohydrates: Elements C, H, O (ratio 1:2:11:2:1). Monomer: Glucose. Sub-types: Starch (amylose/amylopectin), glycogen, cellulose. Roles: Energy storage and support.     - Lipids: Elements C, H, O (ratio C:H approx 1:21:2; high C:O and H:O ratios like 9:19:1 or 18:118:1). Sub-units: Glycerol, fatty acids, phosphate. Examples: Triglycerides, phospholipids. Roles: Energy storage, thermal/electrical insulation, membranes.     - Proteins: Elements C, H, O, N, S. Monomer: Amino acids (2020 different types). Examples: Haemoglobin, collagen, amylase, pepsin, insulin, antibodies. Roles: Transport, support, catalysts, messengers, protection.     - Nucleic Acids: Elements C, H, O, N, P. Monomer: Nucleotides (55 types). Examples: DNA, RNA (mRNAmRNA, tRNAtRNA, rRNArRNA). Roles: Information storage/retrieval, protein production.

Water and Hydrogen Bonding

  • Water (H2O) forms approximately 70%70\% of animal bodies and 90%90\% of plants.
  • The water molecule is dipolar: oxygen is slightly electronegative (δ−\delta-) and hydrogen is slightly electropositive (δ+\delta+). This occurs because oxygen has a greater attraction for covalent bond electrons.
  • Hydrogen bonds form between the negative charge of oxygen on one molecule and the positive charge of hydrogen on another. Each bond is weak (about 1/101/10 the strength of a covalent bond) and frequently breaks/reforms.
  • Properties of Water:     - Solvent: Good for charged substances (ions like Na+Na^+, Cl−Cl^-) and polar molecules (glucose). Carbon dioxide is significantly more soluble than oxygen.     - High Specific Heat Capacity: Requires 4.2 J4.2\,J to increase the temperature of 1 g1\,g of water by 1 ∘C1\,^{\circ}C. This limits temperature fluctuations in organisms.     - High Latent Heat of Vaporisation: High energy needed for evaporation, making transpiration and sweating efficient cooling mechanisms.     - High Latent Heat of Fusion: High energy needed to melt ice; water in cells stays liquid longer to prevent membrane damage from crystals.     - Density: Ice is less dense than water. It acts as insulation for aquatic habitats. Organisms at risk of freezing produce 'anti-freeze' compounds to lower the freezing point of cytoplasm.     - Incompressibility: Provides hydrostatic skeletons (sea anemones, worms) and turgidity in plants.     - Cohesion: Hydrogen bonds hold molecules together, supporting water columns in xylem and creating surface tension.
  • Water Reactions: Water splits into hydrogen ions (H+H^+) and hydroxyl ions (OH−OH^-). It is used in hydrolysis (e.g., digestion) and photosynthesis (provides ions/electrons).

Carbohydrates: Sugars and Polysaccharides

  • Carbohydrates contain C, H, and O with the general formula Cx(H2O)yC_x(H_2O)_y.
  • Simple Sugars (Monosaccharides): Cx(H2O)y where x is 33, 44, 55, 66, or 77.     - Glucose (C6H12O6C_6H_{12}O_6): Exists in ring and straight-chain forms.     - Ring forms of glucose: α\alpha-glucose (hydroxyl −OH-OH group below the ring at C1) and β\beta-glucose (−OH-OH above the ring at C1).     - Hexoses (66 carbons): Glucose, fructose, galactose. Pentoses (55 carbons) are components of nucleotides. Trioses (33 carbons) are metabolic intermediates.
  • Complex Sugars (Disaccharides): Two monosaccharides joined by a covalent glycosidic bond through a condensation reaction (elimination of water).     - Sucrose: Formed from α\alpha-glucose and fructose. It is non-reducing, water-soluble, and polar. Plants use it for transport in phloem because it is less reactive than glucose.     - Hydrolysis: The addition of water to break a glycosidic bond.
  • Polysaccharides: Polymers used for energy storage or structure.     - Starch (Plants): Composed of Amylose (unbranched unbranched 1,41,4 glycosidic bonds, right-handed helix) and Amylopectin (branched, 1,41,4 and 1,61,6 glycosidic bonds).     - Glycogen (Animals/Fungi): Similar to amylopectin but more highly branched (1,41,4 and 1,61,6 bonds).     - Cellulose: Unbranched straight chains of β\beta-glucose (1,41,4 bonds) with alternate molecules rotated 180∘180^{\circ}. projecting −OH-OH groups form hydrogen bonds between chains to create microfibrils. These arrange in a criss-cross pattern for strength in cell walls.

Lipids and Human Health

  • Lipids have much higher H:O ratios than carbohydrates. They are non-polar and insoluble in water.
  • Triglycerides: Glycerol plus three fatty acids joined by ester bonds.     - Saturated fatty acids: No double bonds between carbons in the chain, holding maximum hydrogens.     - Unsaturated fatty acids: At least one double bond between carbons, resulting in fewer hydrogens.     - Efficient for energy storage: Released energy upon oxidation is much higher than carbohydrates/proteins due to high reduction (hydrogen content).
  • Phospholipids: Glycerol, two fatty acids, and a phosphate group (often with choline).     - Structure: Hydrophilic (water-liking) head and two hydrophobic (water-hating) tails.     - In water, they form monolayers, micelles (spheres), or bilayers (the basis of biological membranes).
  • Fat in Diet and Obesity:     - Essential fatty acids: Two types humans cannot synthesize and must consume.     - Fat-soluble vitamins: AA, DD, EE, and KK.     - Energy Balance: Positive balance leads to fat storage. Negative balance results in fat usage.     - Body Mass Index (BMI): BMI=body mass in kg(height in metres)2\text{BMI} = \frac{\text{body mass in kg}}{(\text{height in metres})^2}.     - BMI Categories: Underweight (<20<20), Acceptable (20−2520-25), Overweight (25−3025-30), Obese (>30>30), Very Obese (>40>40).

Proteins and Amino Acids

  • Amino Acid Structure: Central carbon atom attached to an amine group (−NH2-NH_2), a carboxylic acid group (−COOH-COOH), a hydrogen atom, and a residual (RR) group.
  • Key Amino Acids:     - Glycine: Smallest (R is −H-H); allows close packing in collagen.     - Alanine: Non-polar (R is −CH3-CH_3).     - Cysteine: Contains sulfur (R is −CH2−SH-CH_2-SH); forms covalent disulphide bonds.
  • Peptide Bonds: Form between the carbon of the carboxyl group of one amino acid and the nitrogen of the amine group of another.     - <10<10 amino acids: Dipeptide, tripeptide.     - >10>10 amino acids: Polypeptide.
  • Levels of Protein Organisation:     - Primary structure: The specific sequence of amino acids and position of disulphide bonds.     - Secondary structure: Local folding into α\alpha-helices or β\beta-pleated sheets, stabilized by hydrogen bonds between −NH-NH and −CO-CO groups.     - Tertiary structure: Further folding into a complex 3D shape, stabilized by hydrogen bonds, ionic bonds (between ionized R groups), hydrophobic interactions, and disulphide bonds.     - Quaternary structure: Association of two or more polypeptide chains (Identical or different).
  • Globular vs. Fibrous Proteins:     - Globular: Soluble, complex folding, hydrophilic R groups on the surface (e.g., haemoglobin, enzymes).     - Fibrous: Insoluble, simple shapes, high tensile strength (e.g., collagen, keratin).
  • Case Studies:     - Haemoglobin: Globular conjugated protein with four polypeptides (two α\alpha, two β\beta). Each has a prosthetic haem group with an iron atom (Fe2+Fe^{2+}) at the center. Carries four oxygen molecules. Binding of the first oxygen causes an induced fit change from 'tense' to 'relaxed' state.     - Collagen: Three identical left-handed helical polypeptides wound into a triple helix. Glycine occurs every third amino acid. Triple helices are covalently bonded into network fibers (300 nm300\,nm wide) with staggered ends to prevent weakness.

Biochemical Testing Procedures

  • Qualitative Tests:     - Starch: Iodine in potassium iodide solution. Positive: Yellow-orange to blue-black.     - Reducing Sugars: Benedict's solution (alkaline copper sulfate) + heat. Positive: Blue to green/yellow/orange/brick-red precipitate (Cu2+Cu^{2+} reduced to Cu+Cu^+ in copper(I) oxide).     - Non-reducing Sugars (Sucrose): Negative Benedict’s test first. Hydrolyse with dilute HClHCl, boil, neutralize with NaOHNaOH or NaHCO3NaHCO_3, then re-test with Benedict’s. Positive: Blue to red signal.     - Proteins: Biuret reagent (CuSO4CuSO_4 and NaOHNaOH). Positive: Blue to violet/lilac/purple.     - Lipids: Emulsion test (EthanolEthanol + water). Positive: White cloudiness/emulsion.
  • Quantitative Tests:     - Semi-quantitative Benedict's: compare test tube color against established glucose standards (0.10.1 to 50.0 g dm−350.0\,g\,dm^{-3}).     - Quantitative Starch: Prepare starch dilutions (e.g., 0.010.01 to 100 g dm−3100\,g\,dm^{-3}), add iodine, measure optical density using a colorimeter (absorbance or percentage transmission), and plot a calibration graph.

Cell Structure and Microscopy

  • Principles of Microscopy:     - Resolution: The ability to distinguish detail; limited by the wavelength of radiation. Eye resolution is approx 200 μm200\,\mu m.     - Magnification: Ratio of image size to actual size. Magnification=size of imageactual size\text{Magnification} = \frac{\text{size of image}}{\text{actual size}}.
  • Microscope Comparison:     - Light Microscope: Resolution 200 nm200\,nm, max magnification ×1500\times 1500, uses light (400−700 nm400-700\,nm), observes living cells in color.     - Electron Microscope: Resolution 0.5 nm0.5\,nm, max magnification ×250,000\times 250,000, uses electron beams (1.0 nm1.0\,nm), observes dead specimens in a vacuum (black and white images).
  • Eukaryotic Organelles:     - Nucleus: Stores DNA; contains a nucleolus (ribosome production).     - RER: Coated in ribosomes (80S80S); protein synthesis and transport.     - SER: Lacks ribosomes; lipid/cholesterol/phospholipid synthesis.     - Golgi Body: Modifies/packages proteins into vesicles; makes lysosomes.     - Mitochondria: Double membrane, fluid matrix, inner cristae folds; site of aerobic respiration.     - Chloroplasts: Site of photosynthesis (plant cells only); contain chlorophyll.     - Lysosomes: Contain hydrolytic digestive enzymes.     - Centrioles: Assemble spindles for division (animal cells only).     - Cell Wall: Cellulose structure (plant cells only) for support and shape.
  • Prokaryotes vs. Eukaryotes:     - Prokaryotes: 0.5−3.0 μm0.5-3.0\,\mu m, no nucleus (loop of DNA), 70S70S ribosomes, cell wall made of murein (peptidoglycan), may have capsules/flagella.     - Endosymbiosis Theory: Proposes that mitochondria and chloroplasts evolved from bacteria that 'invaded' anaerobic ancestral cells. Evidence: they have their own loop of DNA, 70S70S ribosomes, and similar membrane systems.
  • Tissues and Organs:     - Tissue: Groups of similar cells with the same function (e.g., squamous/columnar epithelium, xylem, phloem).     - Organ: Structures of different tissues performing complex functions (e.g., leaf, liver, heart).

Movement Across Membranes

  • Fluid Mosaic Model: A sea of phospholipids in a bilayer (7−10 nm7-10\,nm wide) with floating transmembrane proteins. Cholesterol stabilizes the bilayer.     - Glycoproteins/Glycolipids: Act as receptors for hormones/neurotransmitters and cell recognition sites.
  • Transport Mechanisms:     - Simple Diffusion: Small/non-polar molecules (oxygen, CO2CO_2, ethanol) pass through the bilayer down a concentration gradient. No energy required.     - Facilitated Diffusion: Polar molecules/ions use channel proteins or carrier proteins to cross the membrane.     - Osmosis: Net movement of water through a partially permeable membrane from high water potential to low water potential.     - Active Transport: Movement against a gradient using carrier proteins and energy (ATPATP) from respiration.     - Bulk Transport: Endocytosis (taking in large particles via vacuoles) and Exocytosis (exporting materials via vesicles fusing with the cell membrane).
  • Water Potential (Ψ\Psi):     - Determined by water quantity and solute concentration. Plant cells have pressure potential (Ψp\Psi_p) exerted by the cell wall.     - Turgid: Cell full of water, membrane pushes against wall. Ψ=0 kPa\Psi = 0\,kPa when fully turgid.     - Plasmolysis: Vacuole shrinks, cytoplasm pulls away from the cell wall in hypertonic (low Ψ\Psi) solutions. Cell is flaccid.

Enzymes: Biological Catalysts

  • Enzymes are globular proteins that lower the activation energy of metabolic reactions. They are specific due to the shape of the active site.
  • Models of Action:     - Lock and Key: Substrate fits exactly into the active site.     - Induced Fit: Enzyme changes shape slightly to mold around the substrate for a tighter fit.
  • Enzyme examples:     - Amylase: Starch →\rightarrow maltose.     - Catalase: 2H2O2→2H2O+O22H_2O_2 \rightarrow 2H_2O + O_2.
  • Factors Influencing Activity:     - Substrate Concentration: Rate increases until active sites are saturated (limiting factor becomes enzyme concentration).     - Temperature: Rate increases with kinetic energy until the optimum (usually approx 40 ∘C40\,^{\circ}C). Above this, vibration breaks bonds, leading to denaturation.     - pH: Each enzyme has an optimum pH (e.g., Pepsin at 1.0−2.01.0-2.0, Catalase at 7.07.0). Deviations cause R-group interaction breakage and denaturation.
  • Inhibition:     - Competitive: Inhibitor has a similar shape to the substrate and competes for the active site. Effect reduced by increasing substrate concentration.     - Non-competitive: Inhibitor binds to an allosteric site, changing the enzyme's overall shape. Effect cannot be overcome by more substrate.

Genetics: DNA, Replication, and Protein Synthesis

  • Nucleic Acids: Polymers of nucleotides. Nucleotides consist of a pentose sugar, a phosphate group, and a nitrogenous base.     - DNA Bases: Adenine, Guanine (purines), Cytosine, Thymine (pyrimidines).     - RNA Bases: Adenine, Guanine, Cytosine, Uracil (UU replaces TT).
  • DNA Structure: Double helix of two antiparallel strands connected by hydrogen bonds (A–T has 22 bonds; C–G has 33). Sugar-phosphate 'backbone' held by phosphodiester bonds.
  • DNA Replication: Semi-conservative process.     - Helicase separates strands; Topoisomerase unwinds.     - DNA Polymerase assembles free nucleotides against template strands in a 5′5' to 3′3' direction.     - Meselsohn and Stahl (1958) proven the semi-conservative nature using nitrogen isotopes.
  • Protein Synthesis:     - Transcription (Nucleus): RNA polymerase makes a complementary mRNAmRNA copy of the DNA template strand. Transcription factors and promoter sequences regulate the process.     - Translation (Ribosomes): mRNAmRNA codons are matched by tRNAtRNA anticodons carrying specific amino acids. Peptidyl transferase (a ribozyme) forms peptide bonds. The genetic code is degenerate (multiple codons per amino acid) and universal.
  • From Gene to Phenotype: Genes code for polypeptides. Faulty genes cause disorders:     - Albinism: Faulty tyrosinase gene (TYRTYR).     - Phenylketonuria (PKUPKU): Faulty phenylalanine hydroxylase gene (PAHPAH).

Cell Division: Mitosis and Meiosis

  • Mitosis: Maintains genetic stability. Stages: Prophase (condensation), Metaphase (equatorial alignment), Anaphase (chromatid separation), Telophase (nuclear reform). Followed by Cytokinesis.
  • Cell Cycle phases: G1G1 (growth), SS (DNA synthesis), G2G2 (growth), and Mitosis (MM).
  • Meiosis: Halves chromosome number for sexual reproduction. Consists of two divisions:     - Meiosis I: Homologous chromosomes pair (Bivalents) and separate. Crossing over occurs at chiasmata.     - Meiosis II: Sister chromatids separate. Produces four genetically different haploid (nn) nuclei.
  • Sources of Variation: Random segregation of chromosomes (2232^{23} combinations in humans) and crossing over.

Inheritance and Genetic Engineering

  • Mendel’s Laws: Law of Segregation (alleles separate) and Law of Independent Assortment (unlinked genes separate independently).
  • Patterns:     - Monohybrid: 3:13:1 ratio in F2F2.     - Dihybrid: 9:3:3:19:3:3:1 ratio in F2F2.     - Codominance: Both alleles expressed (e.g., Mirabilis jalapa flowers: red, white, pink).     - Sex Linkage: Genes on X-chromosome (e.g., Haemophilia, color blindness).     - Multiple Alleles: e.g., ABO blood groups (IAI^A, IBI^B are codominant, IOI^O is recessive).     - Epistasis: Interaction where one gene masks another (e.g., flower color in Collinsia parviflora).9:4:39:4:3 or 9:3:49:3:4 ratios.
  • Chi-Squared (χ2\chi^2) Test: χ2=∑(O−E)2E\chi^2 = \sum \frac{(O-E)^2}{E}. Used to determine if results differ significantly from expected ratios. A value with p<0.05p < 0.05 is significant.
  • Genetic Engineering: Recombinant DNA technology.     - Restriction Enzymes: Cut DNA at palindromic restriction sites (blunt or sticky ends).     - Vector: Transports gene (Plasmids, viruses, liposomes).     - Ligase: Joins DNA fragments.     - Reverse Transcriptase: Makes cDNAcDNA from mRNAmRNA (used for human insulin production).     - Gene Therapy: Transferring functioning genes into patients (e.g., SCID, Cystic Fibrosis).
  • GMO Examples: Bt crops (insect resistance), Herbicide resistance (Soya), Golden Rice (vitamin A precursors), Transgenic animals (antithrombin in goat milk).

Variation, Selection and Speciation

  • Variation Types:     - Discontinuous: Clear categories, monogenic (e.g., blood groups, ear lobe attachment).     - Continuous: Range of phenotypes, polygenic, affected by environment (e.g., height, milk yield).
  • Selection Types:     - Stabilising: Favors the intermediate form (e.g., horseshoe crab, warbler wing length).     - Directional: Favors one extreme due to environmental change (e.g., Darwin’s finches during drought, peppered moth melanism).     - Disruptive: Favors both extremes, selecting against the middle (e.g., African seedcracker beaks).
  • Natural Selection Examples: Kettlewell’s moths (industrial melanism), antibiotic resistance in bacteria (vertical and horizontal transmission), guppies in Trinidad (predation affects maturation size).
  • Mutations: Chromosome mutations (Aneuploidy like Down's Syndrome 2n=472n=47; Polyploidy) and Gene mutations (Substitution, Frameshift, Stutter/repeat).
  • Speciation: Formation of new species.     - Allopatric: Geographical isolation (e.g., snapping shrimps at Isthmus of Panama).     - Sympatric: Within the same area (e.g., polyploidy in Spartina cord grass, Lonicera fly hybrids).

Reproductive Biology

  • Asexual Reproduction: Produces clones. Methods: Binary fission (bacteria), Budding (yeast, Aiptasia), Fragmentation (Spirogyra), Spores (Rhizopus).
  • Plant Sexual Reproduction:     - Pollen produced in anthers (pollen mother cell →meiosis\xrightarrow{meiosis} tetrad).     - Embryo sac in ovule (mother cell →meiosis\xrightarrow{meiosis} 44 cells →3 degenerate\xrightarrow{3\,degenerate} 1\,cell\,\xrightarrow{mitosis}$ 8\,nuclei).\n    - Double Fertilisation: One male gamete fuses with ovum (2nzygote);onefuseswithtwopolarnuclei(zygote); one fuses with two polar nuclei (3n endosperm).\n- Human Reproduction:\n    - Gametogenesis: Spermatogenesis (equal division) and Oogenesis (unequal division; arrested in meiosis I until menstrual cycle).\n    - Fertilisation: Occurs in the oviduct. Involves capacitation, acrosome reaction, and cortical reaction (to prevent polyspermy).\n    - Internal Development: Blastula implants in endometrium. Placenta (maternal/foetal tissue) provides gas exchange, nutrition (glucose by facilitated diffusion), and hormone secretion (hCG, progesterone, oestrogen).
  • Hormonal Control:     - GnRH (Hypothalamus) \rightarrow$$ FSH/LH (Anterior Pituitary).     - Males: Negative feedback of testosterone and inhibin.     - Females: Complex cycle (Follicular, Ovulation, Luteal phases). LH surge triggers ovulation.
  • Maternal Behavior: Alcohol (Foetal Alcohol Syndrome), Nicotine (restricts blood flow/oxygen transport), Carbon monoxide (carboxyhaemoglobin), Folic acid (prevents spina bifida).