Complete CAPE Biology Unit 1 Study Notes: Module 1
BIOLOGY UNIT 1: ASPECTS OF BIOCHEMISTRY
1. Water
The Structure of a Water Molecule
- Molecular Composition: Water (H2O) consists of one oxygen atom covalently bonded to two hydrogen atoms. These are single covalent bonds where oxygen shares one electron with each hydrogen.
- Electron Configuration: Oxygen has six outer-shell electrons. Two are used for bonding, leaving four electrons organized into two non-bonding pairs.
- Polarity and Dipoles: Electrons in the covalent bonds are shared unequally. The oxygen atom pulls electrons toward its nucleus, gaining a small negative charge (δ−), while hydrogen atoms gain small positive charges (δ+). This unequal charge distribution creates a permanent dipole.
- Molecular Geometry: The two hydrogen atoms are positioned on one side of the oxygen atom, creating a V-shape with a bond angle of approximately 104.5∘.
Hydrogen Bonding
- Definition: A weak electrical attraction between the δ+ hydrogen of one water molecule and the δ− oxygen of another.
- Dynamic Nature: In liquid water, these bonds constantly break and reform as molecules move. In ice, each molecule is hydrogen-bonded to four neighbors in a stable lattice.
- Biological Importance: Hydrogen bonds are "long-distance" relative to covalent bonds and are crucial for the structure of proteins and DNA.
States of Water and Density
- Kinetic Energy:
- Ice: Molecules have little kinetic energy, vibrating in fixed positions.
- Liquid Water: Molecules move past each other, forming fleeting bonds.
- Water Vapour: Molecules are far apart with minimal interaction.
- Structure of Ice: As water cools, molecules slow down and form the maximum four hydrogen bonds, creating a rigid, open lattice. This lattice holds molecules further apart than in liquid form.
- Density Anomaly: Water is most dense at 4∘C. Ice is less dense than liquid water and floats. This insulates aquatic life below the surface and prevents bodies of water from freezing solid.
Thermal Properties of Water
- Specific Heat Capacity: The energy required to raise the temperature of 1g of a substance by 1∘C. For water, this is 4.2J/g∘C. High energy is needed to break hydrogen bonds before the temperature can rise, ensuring thermal stability in organisms and aquatic environments.
- Latent Heat of Vaporisation: The energy required to turn liquid into gas. Evaporation of water (like sweat) requires significant heat to break bonds, providing a powerful cooling mechanism for terrestrial organisms.
- Latent Heat of Fusion: The energy required to change water from solid to liquid (300J/g). This high value makes it difficult for cytoplasm to freeze, protecting cells from crystal damage.
Solvent and Chemical Properties
- Solvent Versatility: Water's dipoles attract ions (like Na+ and Cl−) and polar molecules (like glucose). The water molecules surround the solute, breaking ionic bonds or forming new hydrogen bonds to keep them in solution.
- Metabolic Reactions: Most chemical reactions in the body occur in solution so that ions/molecules can come into contact. Water also acts as a reactant in hydrolysis and a product in condensation.
- Cohesion and Surface Tension: Water molecules stick together (cohesion) allowing mass flow in xylem and blood vessels. High surface tension allows small organisms to walk on water.
- pH and Buffering: Pure water dissociates into equal parts H+ and OH−, giving it a neutral pH of 7.0. Biological fluids are often buffered between pH 7 and 8.
2. Carbohydrates
Monosaccharides (Simple Sugars)
- General Formula: (CH2O)n. They are soluble in water and taste sweet.
- Classification by Carbon Number:
- Trioses (3C): e.g., Glyceraldehyde (first carbohydrate in photosynthesis).
- Pentoses (5C): e.g., Ribose (RNA), Deoxyribose (DNA).
- Hexoses (6C): e.g., Glucose, Fructose, Galactose.
- Glucose Structure: Exists in straight-chain or ring forms. Ring formation occurs between C1 and the oxygen on C5.
- α-glucose: The −OH group on C1 is below the ring (opposite side of C6).
- β-glucose: The −OH group on C1 is above the ring (same side as C6).
Disaccharides and the Glycosidic Bond
- Formation: Two monosaccharides link via a condensation reaction (removing H2O) to form a glycosidic bond.
- Common Disaccharides:
- Maltose: α-glucose + α-glucose (α1−4 bond).
- Sucrose: α-glucose + β-fructose (α1−β2 bond). Used for transport in plants.
- Hydrolysis: The breakage of glycosidic bonds by adding water, catalyzed by enzymes like maltase or sucrase.
Polysaccharides (Complex Carbohydrates)
- Definition: Giant polymers made of thousands of monosaccharide monomers. Insoluble and ideal for storage.
- Starch (Plant Storage): Mixture of two polymers:
- Amylose: α1−4 glycosidic bonds; unbranched; coils into a compact spiral via internal hydrogen bonds.
- Amylopectin: α1−4 bonds with α1−6 branches; less compact than amylose.
- Glycogen (Animal Storage): Similar to amylopectin but more highly branched. Stored in liver and muscles; easily mobilized into glucose.
- Cellulose (Structural): Polymer of β-glucose joined by β1−4 bonds. Alternate glucose units are rotated 180∘. This makes the molecule straight. Hydrogen bonds between parallel chains form strong microfibrils and fibers.
Chemical Testing for Carbohydrates
- Benedict's Test (Reducing Sugars): Heated with Benedict's reagent (blue copper(II) sulphate). Reducing sugars (glucose, fructose, maltose) reduce Cu2+ to Cu+, forming a brick-red copper(I) oxide precipitate.
- Non-reducing Sugars (Sucrose): Shows negative Benedict's result. Must be hydrolyzed with acid, neutralized with alkali, and re-tested to show a positive result.
- Iodine Test (Starch): Iodine solution turns blue-black in the presence of amylose.
3. Proteins
Amino Acids
- Basic Structure: A central carbon atom bonded to an amino group (−NH2), a carboxyl group (−COOH), a hydrogen atom, and a variable R-group.
- R-Groups: There are 20 different naturally occurring R-groups. They can be polar (hydrophilic), non-polar (hydrophobic), or sulfur-containing (cysteine).
- Peptide Bonds: Formed via condensation between the amino group of one acid and the carboxyl group of another. The resulting chain is a polypeptide.
Levels of Protein Structure
- Primary Structure: The unique sequence of amino acids in the polypeptide chain, determined by genes.
- Secondary Structure: Local folding into regular patterns held by hydrogen bonds between the C=O of one peptide bond and the N-H of another.
- α-helix: A right-handed spiral.
- β-pleated sheet: Parallel or anti-parallel strands.
- Tertiary Structure: The overall 3D folding of the chain. Stabilized by:
- Hydrogen bonds
- Disulphide bridges: Covalent bonds between cysteine R-groups.
- Ionic bonds: Between charged R-groups.
- Hydrophobic interactions: Non-polar R-groups clustering in the center.
- Quaternary Structure: The association of two or more polypeptide chains (e.g., hemoglobin has four).
Globular vs. Fibrous Proteins
- Globular Proteins (e.g., Hemoglobin): Spherical, soluble, and metabolically active. Hemoglobin contains four polypeptide chains (two α, two β), each with a prosthetic haem group containing iron (Fe2+) to bind oxygen.
- Fibrous Proteins (e.g., Collagen): Long, insoluble, and structural. Collagen consists of three helical polypeptide chains wound like a rope (triple helix). Every third amino acid is glycine. Millions of molecules are cross-linked to form fibrils and fibers with high tensile strength.
4. Lipids
Triglycerides
- Composition: One glycerol molecule bonded to three fatty acids via ester bonds (formed by condensation).
- Saturation:
- Saturated: No carbon-carbon double bonds in the tail; usually solid at room temperature.
- Unsaturated: Contain one or more double bonds (C=C), creating "kinks" that prevent close packing; usually liquid (oils).
- Functions: Highly efficient energy store (2× energy of carbohydrates), thermal insulation, and protection.
Phospholipids and Cell Membranes
- Structure: Glycerol bonded to two fatty acids and one phosphate group.
- Amphipathic Nature: The phosphate "head" is negatively charged and hydrophilic; the fatty acid "tails" are non-polar and hydrophobic.
- Bilayer Formation: In water, they arrange with heads facing outward and tails inward, forming the basis of all biological membranes.
5. Cell Structure and Microscopy
Microscopy Concepts
- Magnification: actual sizeimage size.
- Resolution: The smallest distance between two points that can be distinguished. Limit of resolution is roughly 0.45×wavelength.
- Light Microscope: Uses visible light; max resolution 200nm; max useful magnification ×1400. Can view living specimens.
- Electron Microscope: Uses electron beams; max resolution 0.5nm; max magnification ×300,000. Specimens must be dead and in a vacuum.
Organelles
- Nucleus: Contains chromatin (DNA + histones). The nucleolus produces rRNA.
- Endoplasmic Reticulum (ER): RER (with ribosomes) for protein synthesis; SER for lipid synthesis.
- Golgi Body: Modifies, sorts, and packages proteins into vesicles for secretion (exocytosis).
- Mitochondria: Site of aerobic respiration/ATP production. Features cristae (folds) and a matrix.
- Chloroplasts: Site of photosynthesis. Contains thylakoids (grana) and stroma.
- Lysosomes: Vesicles containing digestive enzymes.
- Centrioles: (Animal only) Organize microtubules for the spindle during division.
- Cell Walls: (Plant only) Made of cellulose microfibrils in a pectin matrix.
6. Cell Division
The Cell Cycle
- Interphase: G1 (growth), S (DNA replication), G2 (prep for mitosis).
- Mitosis: Division of the nucleus into two identical daughter nuclei.
- Prophase: Chromosomes condense; spindle forms.
- Metaphase: Chromosomes align at the equator.
- Anaphase: Centromeres split; chromatids move to poles.
- Telophase: Nuclear envelopes reform.
- Cytokinesis: Division of the cytoplasm.
Meiosis
- Purpose: Reduction division to produce four haploid gametes from one diploid cell.
- Meiosis I: Homologous chromosomes pair (bivalents) and separate. Includes crossing over at Prophase I.
- Meiosis II: Chromatids separate (similar to mitosis).
- Variation Sources: Independent assortment of bivalents and crossing over (chiasmata).
7. Membrane Transport
Passive Transport
- Diffusion: Net movement down a concentration gradient.
- Facilitated Diffusion: Movement through channel or carrier proteins (for ions/polar molecules).
- Osmosis: Diffusion of water through a partially permeable membrane down a water potential (ψ) gradient.
- Water Potential Formula: ψ=ψs+ψp (ψs = solute potential; ψp = pressure potential).
Active processes
- Active Transport: Moving substances against a gradient using ATP and carrier proteins (e.g., Sodium-Potassium pump).
- Bulk Transport: Endocytosis (engulfing) and Exocytosis (secreting) using vesicles.