AP Biology Unit One Notes

Overview of Unit One in AP Biology

  • Instructor Introduction: Mrs. Jones, AP Biology Teacher.

  • Resources Available:

    • Daily review questions on Instagram

    • 374-page review guide on Weebly: www.apoppenguin.weebly.com

    • Weekly "FRQ Friday" videos covering free response questions

    • 120 quizzes and educational games available

    • Additional review PowerPoints on www.apbiopwith.com

Macromolecules Overview

  • Four Key Macromolecules:

    1. Carbohydrates: Sugars and starches.

    2. Proteins: Structural support and enzymes.

    3. Nucleic Acids: Genetic material (DNA, RNA).

    4. Lipids: Fats and membranes.

Carbohydrates

  • Structure of Carbohydrates:

    • Composed of carbon (C), hydrogen (H), and oxygen (O).

    • General formula: CnH2nOnC_{n}H_{2n}O_{n} (1:2:1 ratio).

    • Monomers: Monosaccharides (e.g., glucose -C6H12O6C_6H_{12}O_6).

    • Polymers: Polysaccharides.

  • Types of Carbohydrates:

    • Monosaccharides: Glucose, Fructose, Galactose.

    • Disaccharides: Sucrose (Glucose + Fructose), Lactose (Glucose + Galactose), Maltose (2 Glucose).

    • Bond type: Glycosidic linkages.

    • Polysaccharides:

    • Cellulose: Structural component of plant cell walls.

    • Chitin: Found in fungal cell walls and exoskeletons.

    • Starch: Energy storage in plants.

    • Glycogen: Energy storage in animals (stored in the liver).

  • Differences between Starch and Cellulose:

    • Starch has 1−41-4 alpha linkages (digestible by humans).

    • Cellulose has 1−41-4 beta linkages (indigestible by humans), requiring symbiotic microbes for breakdown.

Proteins

  • Composition: Carbon, Hydrogen, Oxygen, Nitrogen, and Sulfur.

  • Monomer: Amino acids.

  • Amino Acid Structure:

    • Central carbon (C), an amino group (-NH2), a carboxylic acid (-COOH), a hydrogen atom, and a variable R group (side chain).

  • Types of Bonds:

    • Peptide bonds between amino acids (formed between the amino group of one and the carboxy group of another).

  • Levels of Protein Structure:

    1. Primary Structure: Sequence of amino acids.

    2. Secondary Structure: Alpha-helix and beta-pleated sheets (stabilized by hydrogen bonds).

    3. Tertiary Structure: Overall 3D shape (stabilized by various bonds and interactions).

    4. Quaternary Structure: Assembly of multiple polypeptide chains (e.g., Hemoglobin).

  • Protein Folding:

    • R groups (side chains) play a critical role in determining protein structure; hydrophilic R groups are on the surface, hydrophobic R groups are buried inside.