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Biomolecules: Structure, Function, and Classification

Study Guide - Smart Notes

Tailored notes based on your materials, expanded with key definitions, examples, and context.

Unit 2: Biomolecules

Atomic Structure of Carbon

Carbon is a fundamental element in biological molecules due to its unique atomic structure and bonding capabilities.

  • Atomic Structure: Carbon has an atomic number of 6, with 4 electrons in its outer shell, allowing it to form up to four covalent bonds.

  • Bonding: Carbon typically forms single, double, or triple covalent bonds with other atoms, including hydrogen, oxygen, nitrogen, and other carbons.

  • Versatility: The ability to form chains, rings, and complex structures makes carbon the backbone of organic molecules.

  • Example: Methane (CH4) demonstrates carbon's ability to form four single covalent bonds.

Polymer Formation and Breakdown

Polymers are large molecules composed of repeating subunits called monomers. Their synthesis and degradation are essential biological processes.

  • Dehydration Synthesis: Polymers are built by joining monomers through the removal of water molecules.

  • Hydrolysis: Polymers are broken down into monomers by the addition of water.

  • Equation:

  • Example: Formation of starch from glucose monomers.

Carbohydrates: Structure and Function

Carbohydrates are organic molecules composed of carbon, hydrogen, and oxygen, serving as energy sources and structural components.

  • Monosaccharides: Simple sugars (e.g., glucose, fructose, galactose) with the general formula .

  • Disaccharides: Two monosaccharides joined by a glycosidic bond (e.g., sucrose, lactose, maltose).

  • Polysaccharides: Long chains of monosaccharides (e.g., starch, glycogen, cellulose).

  • Functions: Energy storage (starch, glycogen), structural support (cellulose in plants).

Type

Structure

Examples

Function

Monosaccharide

Single sugar unit

Glucose, Fructose

Quick energy

Disaccharide

Two sugar units

Sucrose, Lactose

Transport, energy

Polysaccharide

Many sugar units

Starch, Cellulose

Storage, structure

Lipids: Structure and Function

Lipids are hydrophobic molecules important for energy storage, membrane structure, and signaling.

  • Triglycerides: Composed of three fatty acids and one glycerol; main form of stored energy.

  • Steroids: Four fused carbon rings; includes hormones like cholesterol and testosterone.

  • Phospholipids: Two fatty acids, one glycerol, and a phosphate group; major component of cell membranes.

  • Functions: Energy storage, membrane structure, signaling.

Lipid Type

Structure

Example

Function

Triglyceride

Glycerol + 3 fatty acids

Fats, oils

Energy storage

Steroid

4 fused rings

Cholesterol

Hormones, membrane fluidity

Phospholipid

Glycerol + 2 fatty acids + phosphate

Phosphatidylcholine

Cell membrane

Saturated vs. Unsaturated Fatty Acids

Fatty acids differ in the presence or absence of double bonds, affecting their physical properties and health implications.

  • Saturated Fatty Acids: No double bonds; straight chains; solid at room temperature (e.g., butter).

  • Unsaturated Fatty Acids: One or more double bonds; bent chains; liquid at room temperature (e.g., olive oil).

  • Health: Unsaturated fats are generally considered healthier than saturated fats.

Type

Bonding

Physical State

Example

Saturated

No double bonds

Solid

Butter

Unsaturated

One or more double bonds

Liquid

Olive oil

Amino Acids: Structure and Diversity

Amino acids are the building blocks of proteins, each with a central carbon, amino group, carboxyl group, hydrogen, and a unique R group.

  • General Structure:

  • R Group: The side chain (R group) distinguishes the 20 different amino acids, affecting their properties and functions.

  • Classification: Amino acids can be polar, nonpolar, acidic, or basic.

  • Example: Glycine has a hydrogen as its R group; glutamic acid has a carboxyl group.

Proteins: Structure and Function

Proteins are polymers of amino acids that perform a wide range of functions in living organisms.

  • Primary Structure: Sequence of amino acids.

  • Secondary Structure: Local folding (alpha helix, beta sheet) due to hydrogen bonding.

  • Tertiary Structure: Overall 3D shape formed by interactions among R groups.

  • Quaternary Structure: Association of multiple polypeptide chains.

  • Functions: Enzymes, structural support, transport, signaling.

  • Example: Hemoglobin (oxygen transport), collagen (structural protein).

Types of Proteins and Their Functions

Proteins are classified based on their roles in the cell and organism.

  • Enzymes: Catalyze biochemical reactions (e.g., amylase).

  • Structural Proteins: Provide support (e.g., keratin, collagen).

  • Transport Proteins: Move substances (e.g., hemoglobin).

  • Signaling Proteins: Hormones and receptors (e.g., insulin).

Protein Type

Example

Function

Enzyme

Amylase

Catalyzes starch breakdown

Structural

Collagen

Connective tissue support

Transport

Hemoglobin

Oxygen transport

Signaling

Insulin

Regulates blood sugar

Identifying Molecules from Structural Formulas

Understanding molecular structures is essential for identifying biomolecules and verifying their correctness.

  • Carbon: Forms 4 bonds.

  • Hydrogen: Forms 1 bond.

  • Oxygen: Forms 2 bonds.

  • Application: Use these rules to check the validity of molecular diagrams.

  • Example: Glucose structure should show each carbon with four bonds.

Additional info: Academic context and examples have been expanded for clarity and completeness.

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