Edexcel (B) Biology A-level - Topic 1: Biological Molecules Study Guide

Carbohydrates Overview

  • Definition: Carbohydrates are biological molecules consisting exclusively of carbon, hydrogen, and oxygen.

  • Basic Structure: They are characterized as long chains of sugar units referred to as saccharides.

  • Classification of Saccharides:     * Monosaccharide: A single sugar monomer.     * Disaccharide: A molecule composed of two monosaccharides.     * Polysaccharide: A complex molecule composed of many monosaccharides.

  • Bonding and Formation: Monosaccharides join to form disaccharides and polysaccharides through the formation of glycosidic bonds, which occur during condensation reactions.

Monosaccharides: Structure and Examples

  • Glucose:     * Contains six carbon atoms in each molecule (C6H12O6C_6H_{12}O_6).     * Function: It serves as the primary substrate for respiration.     * Isomers: Glucose exists as two isomers, alpha- (α\alpha) and beta- (β\beta) glucose, which differ in their structural arrangements.

  • Ribose:     * A pentose sugar containing five carbon atoms (C5H10O5C_5H_{10}O_5).     * Function: It is a vital component of RNA.

  • Deoxyribose:     * An isomer of ribose found in DNA.     * Distinction: It lacks the hydroxyl (OHOH) group on the second carbon of the sugar ring.

Disaccharides and Formation

  • Disaccharides are formed by the condensation of two monosaccharides:     * Maltose: Formed by the condensation of two glucose molecules.     * Sucrose: Formed by the condensation of one glucose molecule and one fructose molecule.     * Lactose: Formed by the condensation of one glucose molecule and one galactose molecule.

Polysaccharides: Storage and Structure

Polysaccharides are formed from many glucose units joined together. Major types include:

  • Glycogen:     * Main energy storage molecule in animals.     * Composition: Many α\alpha-glucose molecules joined by 1,41,4 and 1,61,6 glycosidic bonds.     * Structure: Highly branched with a large number of side branches.     * Properties: The branching allows it to be hydrolysed rapidly for quick energy release. It is a large yet compact molecule, maximizing energy storage density.

  • Starch:     * Primary energy storage in plants, consisting of a mixture of two polysaccharides:     * Amylose: An unbranched chain of glucose molecules joined by 1,41,4 glycosidic bonds. Its structure is coiled and very compact, enabling high-density energy storage.     * Amylopectin: Composed of glucose molecules joined by 1,41,4 and 1,61,6 glycosidic bonds. It is a branched molecule. The numerous side branches allow it to be digested rapidly by enzymes for quick energy release. While compact, it is less so than amylose.

  • Cellulose:     * A structural component of plant cell walls.     * Composition: Long, unbranched chains of β\beta-glucose monomers joined by 1,41,4 glycosidic bonds.     * Structural Organization: Multiple cellulose chains are held together by hydrogen bonds to form strong threads called microfibres and microfibrils, which provide high tensile strength and structural support.

Lipids: Types and Physical Properties

  • Solubility: Lipids are biological molecules only soluble in organic solvents, such as alcohols.

  • Saturated Lipids:     * Found typically in animal fats.     * Chemical Structure: Contain only carbon-carbon single bonds (CCC-C).     * Physical State: Solid at room temperature because the straight chains (without kinks) allow molecules to pack close together.

  • Unsaturated Lipids:     * Commonly found in plants.     * Chemical Structure: Contain carbon-carbon double bonds (C=CC=C).     * Physical State: Liquid at room temperature (oils) because the double bonds create "kinks" in the chain, preventing close packing and resulting in weaker intermolecular forces and a lower melting point.

Functional Properties of Lipids

  • Waterproofing: Fatty tails are hydrophobic, making lipids effective waterproof barriers.

  • Energy Density: Lipids are very compact and offer better gram-for-gram energy release than carbohydrates or proteins. This is because more COC-O bonds are hydrolysed during metabolism.

  • Storage: Being non-polar and insoluble in water, lipids do not interfere with water-based reactions in the cytoplasm, making them ideal for long-term storage.

  • Thermal Insulation: Lipids conduct heat slowly, providing an effective insulation layer for organisms.

Lipid Varieties: Triglycerides and Phospholipids

  • Triglycerides:     * Composition: One molecule of glycerol joined to three fatty acids.     * Bonding: Formed via ester bonds during condensation reactions.     * Variability: Fatty acid chains vary in length and the presence of single or double carbon bonds.     * Function: Used as energy reserves in both plant and animal cells.

  • Phospholipids:     * Structure: Similar to a triglyceride, but one fatty acid is substituted by a phosphate-containing group.     * Amphipathic Nature: The phosphate head is hydrophilic (attracts water), and the fatty acid tails are hydrophobic (repels water).     * Arrangement: They form a bilayer in cell membranes; heads point outward toward the aqueous environment, and tails point inward, away from the water.

Protein Structure and Amino Acids

  • Amino Acids: The monomers of proteins.     * General Structure: Consist of an amino group (NH2NH_2), a carboxyl group (COOHCOOH), and a variable RR group.     * Diversity: There are 2020 different amino acids, each distinguished by its unique RR group, which determines its chemical properties.

  • Bonding: Amino acids join via peptide bonds formed in condensation reactions.     * Dipeptide: Two amino acids joined.     * Polypeptide: Three or more amino acids joined.

  • Levels of Protein Structure:     * Primary Structure: The specific linear sequence of amino acids in the polypeptide chain, maintained by peptide bonds.     * Secondary Structure: The folding of the chain into an α\alpha-helix or β\beta-pleated sheet, stabilized exclusively by hydrogen bonds (electrostatic attraction between oxygen/nitrogen/fluorine and electron-deficient hydrogen).     * Tertiary Structure: The complex 3D folding of the secondary structure. It is maintained by hydrogen bonds, ionic bonds (salt bridges between oppositely charged RR groups), and disulphide bridges (covalent bonds between sulphur atoms in cysteine).     * Quaternary Structure: The 3D arrangement and interaction of more than one polypeptide chain.

Classification of Proteins: Fibrous vs. Globular

  • Fibrous Proteins:     * Consist of long parallel polypeptides with very little tertiary or quaternary structure (mainly secondary).     * Feature occasional cross-linkages to form microfibres for high tensile strength.     * Property: Insoluble in water.     * Function: Used for structural purposes.     * Example (Collagen): High tensile strength due to numerous hydrogen bonds. Composed of three distinct α\alpha-chains forming a triple gamma helix. These link into fibrils and fibres to form bones, cartilage, connective tissue, and tendons.

  • Globular Proteins:     * Possess complex tertiary and quaternary structures.     * Property: Form colloids in water (soluble).     * Function: Diverse roles including hormones and antibodies.     * Example (Haemoglobin): A water-soluble protein made of four polypeptide chains (two α\alpha and two β\beta). Each subunit has a prosthetic haem group containing an Fe2+Fe^{2+} ion. Its function is to bind oxygen and transport it to tissues for respiration.

Nucleic Acids: DNA and RNA

  • Nucleic acids are polymers of nucleotides.

  • Nucleotide Structure: Composed of a pentose (5-carbon sugar), a nitrogen-containing organic base, and a phosphate group.

  • DNA Nucleotides:     * Sugar: Deoxyribose.     * Bases: Adenine (AA), Cytosine (CC), Guanine (GG), or Thymine (TT).

  • RNA Nucleotides:     * Sugar: Ribose.     * Bases: Adenine (AA), Cytosine (CC), Guanine (GG), or Uracil (UU).

  • Base Classification:     * Purines: Adenine and Guanine; these have two nitrogen-containing rings.     * Pyrimidines: Cytosine, Thymine, and Uracil; these are smaller and have a single nitrogen-containing ring.

  • Bonding: Nucleotides are linked by phosphodiester bonds formed in condensation reactions.

  • Double Helix Structure: DNA consists of two polynucleotide strands joined by hydrogen bonds between complementary bases:     * Adenine pairs with Thymine (2 hydrogen bonds).     * Cytosine pairs with Guanine (3 hydrogen bonds).

  • RNA Characteristics: Usually single-stranded and exists in forms such as mRNAmRNA (messenger), tRNAtRNA (transfer), and rRNArRNA (ribosomal).

Semi-Conservative DNA Replication

This process ensures genetic continuity between generations of cells. Steps include:

  1. Unwinding: The DNA double helix unwinds as hydrogen bonds between bases are broken, catalysed by DNA helicase.

  2. Templating: One strand acts as a template. Free nucleotides align via complementary base pairing.

  3. Joining: Adjacent nucleotides are joined by phosphodiester bonds through condensation reactions, catalysed by DNA polymerase.

  4. Re-folding: New molecules fold into double helices as hydrogen bonds form. The resulting DNA contains one original (parental) strand and one newly-synthesised strand.

The Genetic Code

  • Definition: A sequence of bases on DNA that codes for a sequence of amino acids in a polypeptide.

  • Codons: Triplets of bases that each code for a specific amino acid.

  • Genomic Regions:     * Exons: Coding regions of DNA.     * Introns: Non-coding regions.

  • Key Features of the Code:     * Non-overlapping: Each triplet is read once; bases are not shared between adjacent triplets.     * Degenerate: More than one triplet can code for the same amino acid, reducing the impact of mutations like substitutions.     * Universal: The code is identical in all species and organisms.     * Start and Stop: Contains specific codons to initiate or terminate protein synthesis.

  • Mutations:     * Changes in the base sequence (deletions, insertions, substitutions).     * Sickle Cell Anaemia: A mutation that distorts haemoglobin and red blood cell shape.     * Frameshift: Caused by deletions or insertions, where all subsequent codons downstream are misread.

Protein Synthesis: Transcription and Translation

  • Transcription (Nucleus):     1. DNA helicase uncoils DNA and breaks hydrogen bonds.     2. The antisense strand acts as a template; the sense strand is the coding strand.     3. Free nucleotides align and RNA polymerase joins them with phosphodiester bonds to form mRNAmRNA.     4. mRNAmRNA exits through a nuclear pore to reach a ribosome.

  • Translation (Ribosomes on Rough ER):     1. mRNAmRNA attaches to a ribosome. A tRNAtRNA molecule with a specific amino acid binds to the mRNAmRNA via its anticodon.     2. Hydrogen bonds form between the tRNAtRNA anticodon and the mRNAmRNA codon.     3. A second tRNAtRNA binds to the next codon; the two amino acids form a peptide bond.     4. The process repeats, creating a polypeptide chain until a stop codon is reached.

Enzymes and Kinetics

  • Definition: Biological catalysts that lower the activation energy of reactions (anabolic, catabolic, intracellular, or extracellular).

  • Active Site: The specific area where a substrate binds.

  • Induced Fit Model: The enzyme's structure is distorted as the substrate binds, molding the active site around the substrate to form an enzyme-substrate complex.

  • Measurement: Initial rate of reaction is found by calculating the gradient of a concentration-time graph at t=0t=0.

  • Factors Affecting Rate:     * Enzyme Concentration: Rate increases as more active sites become available until substrate concentration becomes the limiting factor.     * Substrate Concentration: Rate increases as more complexes form until enzyme concentration becomes the limiting factor (all active sites saturated).     * Temperature: Rate increases up to an optimum temperature. Beyond this, enzymes denature as hydrogen bonds are broken.

Enzyme Inhibition

  • Competitive Inhibition: Inhibitor molecules compete with the substrate for the active site. This can be reversed by increasing substrate concentration.

  • Non-competitive Inhibition: Inhibitor binds to an allosteric site (different from the active site), changing the enzyme's shape and preventing substrate binding. This cannot be reversed by increasing substrate concentration.

  • Feedback Inhibition: Also known as end-product inhibition, where the final product of a pathway inhibits the enzyme responsible for the initial stage.

Inorganic Ions in Plants

  • Nitrate Ions: Required for synthesis of DNA and amino acids.

  • Calcium Ions: Needed for calcium pectate in the middle lamellae of plant cell walls.

  • Phosphate Ions: Essential for ADP, ATP, DNA, and RNA.

  • Magnesium Ions: Necessary for the production of chlorophyll.

Properties of Water

  • Polarity: Uneven charge distribution (electronegative oxygen vs. electropositive hydrogen). This allows ionic substances like NaClNaCl to dissolve.

  • Polar Solvent: Acts as a medium for metabolic reactions.

  • High Specific Heat Capacity: Requires significant energy to change temperature, minimizing fluctuations and protecting aquatic environments.

  • Latent Heat of Vaporisation: High energy requirement for evaporation provides cooling (e.g., sweating) with minimal water loss.

  • Cohesion and Adhesion: Cohesion (sticking together via hydrogen bonds) allows transport through xylem and high surface tension. Adhesion allows water to stick to cell walls.

  • Density: Maximum density occurs at 4C4\,^{\circ}\text{C}. Ice is less dense and floats, creating an insulating layer on bodies of water that prevents freezing of the entire habitat.

  • Incompressibility: Provides physical support and is useful in hydraulic mechanisms in organisms.