Chapter 5: Organic Molecules

Biological Organic Molecules

  • The four main classes of biological macromolecules:

    1. Carbohydrates – Sugars and polymers of sugars.

    2. Lipids – Fats, phospholipids, and steroids (hydrophobic molecules).

    3. Proteins – Polymers of amino acids.

    4. Nucleic Acids – DNA & RNA.

  • Three of these (Carbohydrates, Proteins, and Nucleic Acids) are polymers, meaning they are made up of monomers linked together.

Dehydration Reaction & Hydrolysis

  • Dehydration Reaction:

    • Builds polymers by linking monomers through the removal of a water molecule.

    • Example: Forming a disaccharide from two monosaccharides.

  • Hydrolysis:

    • Breaks down polymers into monomers by adding a water molecule.

    • Example: Breaking down starch into glucose.

Carbohydrates

Monosaccharides (Simple Sugars)

  • Basic formula: (CH₂O)n.

  • Example from lecture: Glucose (C₆H₁₂O₆).

  • Structure: Can exist in linear or ring form (ring is more stable in water).

  • Functions:

    • Fuel for cells.

    • Raw material for building molecules.

Disaccharides & Polysaccharides

  • Disaccharides:

    • Formed by a dehydration reaction between two monosaccharides.

    • Bond type: Glycosidic linkage.

    • Example: Sucrose (Glucose + Fructose).

  • Polysaccharides:

    • Large polymers of sugars with storage or structural functions.

Polysaccharides & Their Functions

  1. Glycogen:

    • Storage polysaccharide in animals.

    • Stored in liver and muscle cells.

  2. Cellulose:

    • Structural polysaccharide in plants (major component of cell walls).

    • Special Feature: Humans can’t digest cellulose (passes as fiber).

    • Glycosidic bond difference: Cellulose has β-glucose linkages, while starch has α-glucose linkages.

  3. Starch:

    • Storage polysaccharide in plants.

    • Stored in chloroplasts.

    • Example: Amylose (simplest starch).

  4. Chitin:

    • Structural polysaccharide in fungal cell walls & arthropod exoskeletons (insects, crabs).

Lipids (Hydrophobic Molecules)

Characteristics & Examples

  • Lipids do not mix with water (hydrophobic).

  • Three major types:

    1. Fats (Triacylglycerols)

    2. Phospholipids

    3. Steroids

Fats (Triacylglycerols)

  • Structure:

    • Made of 1 glycerol + 3 fatty acids.

    • Linked by ester bonds.

  • Function in Animals:

    • Energy storage.

    • Cushioning & insulation for organs.

Saturated vs. Unsaturated Fats

  • Saturated fats:

    • No double bonds between carbon atoms.

    • Solid at room temperature (ex: butter, animal fats).

  • Unsaturated fats:

    • One or more double bonds (causes bending).

    • Liquid at room temperature (ex: oils).

Hydrogenation

  • Process of adding hydrogen to unsaturated fats to make them saturated.

  • Creates trans fats, which are linked to heart disease.

Phospholipids

  • Structure:

    • Glycerol + 2 fatty acids + phosphate group.

    • Has a hydrophilic head (phosphate) and hydrophobic tails (fatty acids).

  • Significance:

    • Forms the phospholipid bilayer in cell membranes.

Steroids (Cholesterol & Hormones)

  • Structure: Four fused carbon rings.

  • Examples:

    • Cholesterol – Essential for cell membranes but high levels lead to heart disease.

    • Hormones – Testosterone & Estrogen are steroid-based.

Proteins

Polypeptides & Amino Acids

  • Proteins are made of one or more polypeptides.

  • Amino acids:

    • Contain Amino (-NH₂), Carboxyl (-COOH), and R-group (side chain).

    • 20 different types classified as polar, nonpolar, or charged.

Polypeptide Bonds

  • Amino acids are linked by peptide bonds through dehydration reactions.

  • Form long chains (polypeptides).

Levels of Protein Structure

  1. Primary Structure:

    • Sequence of amino acids.

    • Determines final protein shape.

  2. Secondary Structure:

    • Hydrogen bonds create α-helices and β-sheets.

  3. Tertiary Structure:

    • 3D shape formed by interactions between R-groups.

    • Includes hydrogen bonds, disulfide bridges, hydrophobic interactions.

  4. Quaternary Structure:

    • Multiple polypeptide chains combine.

• • Example: Hemoglobin (carries oxygen in blood).