Chapter: The Chemical Basis of Life

This chapter explores the fundamental building blocks of living organisms, moving from simple inorganic molecules to the complex organic structures that form the architecture of the cell.


1. Biological Molecules: Inorganic vs. Organic Compounds

All matter in the universe is composed of atoms, but in biology, we categorize the resulting compounds based on their chemical complexity and the presence of carbon.

Inorganic Compounds

Inorganic compounds are generally simple, small, and lack carbon-hydrogen (C-H) bonds. Although some contain carbon (like carbon dioxide, \(CO_2\)) or hydrogen (like water, \(H_2O\)), they do not contain both. * Examples: Water, mineral salts (e.g., \(NaCl\)), acids, bases, and gases like \(O_2\) and \(CO_2\). * Biological Role: They serve as solvents, reactants in metabolic pathways, and structural components (e.g., calcium phosphate in bones).

Organic Compounds

Organic compounds are defined by the presence of carbon atoms covalently bonded to hydrogen. Carbon’s ability to form four stable covalent bonds allows it to build complex, diverse “backbones” for life. * The Four Classes: Carbohydrates, Lipids, Proteins, and Nucleic Acids. * Properties: They are often large macromolecules (polymers) built from smaller repeating units (monomers) through dehydration synthesis (removal of water to form a bond).

[Figure 1: Comparison of Compounds] Description: A two-part diagram. On the left, simple inorganic molecules like \(H_2O\) and \(NaCl\) (ionic lattice). On the right, a complex organic molecule like Glucose (\(C_6H_{12}O_6\)) highlighting the C-C and C-H covalent backbone.


7.2 Carbohydrates: The Energy and Structural Scaffold

Carbohydrates are composed of Carbon, Hydrogen, and Oxygen, typically in a 1:2:1 ratio (\(CH_2O)_n\). They are categorized by the number of sugar units they contain.

A. Monosaccharides (Simple Sugars)

These are the monomers (single units) of carbohydrates. They typically contain 3 to 7 carbons. * Glucose (\(C_6H_{12}O_6\)): The primary energy source for cellular respiration. It exists as a straight chain or a more stable ring structure in aqueous solutions. * Fructose & Galactose: Isomers of glucose (same formula, different arrangement), found in fruits and milk. * Ribose & Deoxyribose: 5-carbon sugars (pentoses) that form the backbone of RNA and DNA.

B. Disaccharides (Double Sugars)

Formed when two monosaccharides join via a glycosidic bond through a condensation reaction. * Sucrose (Table Sugar): Glucose + Fructose. * Lactose (Milk Sugar): Glucose + Galactose. * Maltose (Malt Sugar): Glucose + Glucose.

C. Polysaccharides (Complex Carbohydrates)

Long chains of hundreds or thousands of monosaccharides. 1. Storage Polysaccharides: * Starch: Glucose storage in plants (found in seeds and tubers). * Glycogen: Glucose storage in animals (highly branched, stored in liver and muscle). 2. Structural Polysaccharides: * Cellulose: Forms the rigid cell wall of plants. Humans cannot digest it (fiber). * Chitin: Found in the exoskeletons of insects and the cell walls of fungi.

[Figure 2: Carbohydrate Structures] Description: A series of three diagrams: (1) A hexagonal glucose ring. (2) Two glucose rings joined by an oxygen bridge (glycosidic bond) to form maltose. (3) A long, branched chain of glucose units representing glycogen.


7.3 Lipids and Proteins

Lipids: Hydrophobic Molecules

Lipids are a diverse group of non-polar molecules that do not dissolve in water. * Triglycerides (Fats and Oils): Composed of one glycerol and three fatty acids. * Saturated: No double bonds; straight chains pack tightly (solid at room temp, like butter). * Unsaturated: One or more double bonds create “kinks”; cannot pack tightly (liquid, like olive oil). * Phospholipids: Composed of glycerol, two fatty acids (hydrophobic tails), and a phosphate group (hydrophilic head). These are the fundamental components of cell membranes. * Steroids: Composed of four fused carbon rings (e.g., Cholesterol, Testosterone).

Proteins: The Molecular Machines

Proteins are polymers of amino acids joined by peptide bonds. There are 20 different amino acids, each with a unique “R-group” (side chain).

The Four Levels of Protein Structure:

  1. Primary (\(1^\circ\)): The linear sequence of amino acids (the “alphabet”).
  2. Secondary (\(2^\circ\)): Local folding into alpha-helices or beta-pleated sheets held by hydrogen bonds between the backbone.
  3. Tertiary (\(3^\circ\)): The overall 3D shape of a single polypeptide, stabilized by R-group interactions (ionic bonds, disulfide bridges, hydrophobic interactions).
  4. Quaternary (\(4^\circ\)): Multiple polypeptide chains (subunits) working together (e.g., Hemoglobin).

[Figure 3: Protein Folding] Description: A flow diagram showing (1) a bead-like chain for primary structure, (2) a spiral ribbon for alpha-helix, (3) a globule for tertiary, and (4) four intertwined globules for quaternary structure.


7.4 Water: The Solvent of Life

Water is polar because oxygen is more electronegative than hydrogen, creating partial charges (\(\delta-\) on O, \(\delta+\) on H). This leads to hydrogen bonding.

  • Cohesion & Adhesion: Water sticks to itself (cohesion) and other surfaces (adhesion), allowing it to travel up plant stems.
  • High Specific Heat: Water absorbs a lot of heat with minimal temperature change, stabilizing internal body temperatures.
  • Solvent Properties: It dissolves polar and ionic substances (“Universal Solvent”), enabling chemical reactions in the cytoplasm.
  • Density of Ice: Water expands when it freezes; ice floats, insulating the life in the water below.

7.5 Enzymes: Biological Catalysts

Enzymes are usually proteins that speed up chemical reactions by lowering the activation energy.

  1. Mechanism: A specific substrate binds to the enzyme’s active site (the “Induced Fit” model). They form an Enzyme-Substrate (ES) Complex, the reaction occurs, and the products are released.
  2. Factors Affecting Activity:
    • Temperature: Low temp slows molecules; high temp denatures (unfolds) the enzyme.
    • pH: Extreme pH disrupts R-group bonds, leading to denaturation.
  3. Inhibition:
    • Competitive: An inhibitor mimics the substrate and blocks the active site.
    • Non-competitive: An inhibitor binds to an allosteric site, changing the enzyme’s overall shape so the substrate no longer fits.

[Figure 4: Enzyme Inhibition] Description: Two panels. Panel A shows a “wrong” molecule blocking the active site (Competitive). Panel B shows a molecule binding to the side of the enzyme, causing the active site to collapse (Non-competitive).


7.6 Plasma Membrane: The Gatekeeper

The membrane is described by the Fluid Mosaic Model. It is “fluid” because molecules move laterally, and “mosaic” because it is a mixture of various components.

Components:

  • Phospholipid Bilayer: Forms the semi-permeable barrier. Only small, non-polar molecules (like \(O_2\)) pass easily.
  • Cholesterol: Wedged between phospholipids to act as a “fluidity buffer”—prevents the membrane from becoming too rigid in the cold or too fluid in the heat.
  • Proteins:
    • Integral (Transmembrane): Transport channels or pumps.
    • Peripheral: Found on the surface; often used for signaling.
  • Carbohydrates (Glycolipids/Glycoproteins): Attached to the exterior; act as “ID tags” for cell-to-cell recognition.

[Figure 5: The Fluid Mosaic Model] Description: A cross-section of the membrane showing a bilayer of “heads and tails.” Large blue protein “icebergs” are embedded. Cholesterol yellow rings are between tails, and green sugar chains sprout from the top surface like antennae.