AP BIO SEM 1
Biological Macromolecules
Carbohydrates
Monomer: Monosaccharides (e.g., glucose, fructose)
Polymer: Polysaccharides (e.g., starch, glycogen, cellulose)
Functions:
Short-term energy storage (e.g., glucose)
Structural support (e.g., cellulose in plants, chitin in arthropods)
Energy storage (e.g., starch in plants, glycogen in animals)
Functional Groups: Hydroxyl (-OH) and Carbonyl (C=O)
Lipids
Monomer: Glycerol and fatty acids (not true monomers)
Polymer: Triglycerides, phospholipids, and steroids
Functions:
Long-term energy storage (triglycerides)
Membrane structure (phospholipids)
Hormones and signaling (steroids like cholesterol)
Insulation and protection
Functional Groups: Carboxyl (-COOH), Hydroxyl (-OH), Methyl (-CH3)
Proteins
Monomer: Amino acids (20 types)
Polymer: Polypeptides (fold into proteins)
Functions:
Enzymes (catalysts for reactions)
Structural (e.g., keratin, collagen)
Transport (e.g., hemoglobin)
Signaling (e.g., insulin)
Defense (e.g., antibodies)
Movement (e.g., actin and myosin)
Functional Groups: Amino (-NH2) and Carboxyl (-COOH) + ADD MORE FUNCTIONAL GROUPS!!
Nucleic Acids
Monomer: Nucleotides (phosphate group, sugar, nitrogenous base)
Polymer: DNA (double-stranded), RNA (single-stranded)
Functions:
Store genetic information (DNA)
Transmit genetic information (RNA)
Energy transfer (ATP)
Functional Groups: Phosphate (-PO4), Hydroxyl (-OH)
Why is Carbon Important for Living Things?
Carbon has 4 valence electrons and can form up to 4 covalent bonds, allowing for complex molecules->tetravalent!!!!.
It can bond with itself to create chains, rings, and diverse structures.
This versatility is essential for the formation of macromolecules (carbs, lipids, proteins, nucleic acids).
Starch vs. Glycogen
Starch: Energy storage in plants; linear or branched chains of glucose (amylose and amylopectin). Alpha Glucose
Glycogen: Energy storage in animals; highly branched chains of glucose for rapid energy release. Beta Glucose
Hydrolysis and Dehydration Synthesis
Hydrolysis: Adds water (H₂O) to break polymers into monomers. Example: Breaking starch into glucose.
Dehydration Synthesis: Removes water to form bonds between monomers, creating polymers. Example: Forming a polypeptide from amino acids.
Covalent Bonds
Polypeptide Formation: Peptide bonds (between amino group and carboxyl group of amino acids).
Nucleic Acid Formation: Phosphodiester bonds (between phosphate group and sugar in nucleotides).
Protein Structure
Primary Structure: Sequence of amino acids (covalent peptide bonds).
Secondary Structure: Coiling or folding due to hydrogen bonds (e.g., α-helices, β-sheets).
Tertiary Structure: 3D shape due to interactions:
Hydrophobic interactions
Hydrogen bonds
Ionic bonds
Disulfide bridges (covalent bonds between cysteine residues)
Quaternary Structure: Two or more polypeptides interacting (e.g., hemoglobin).
Shape Specificity in Protein Function
Proteins function based on their shape, which allows specific interactions.
Example:
Enzymes: Active site binds substrates (lock-and-key or induced fit).
Hemoglobin: Specifically binds oxygen molecules.
Energy Storage in Molecules
Energy is stored in the chemical bonds of molecules, particularly in covalent bonds (e.g., C-H bonds in glucose).
ATP stores energy in its phosphate bonds.
Laws of Thermodynamics
First Law: Energy cannot be created or destroyed; it can only change forms.
Example: Energy in food is converted to ATP.
Second Law: Every energy transfer increases entropy (disorder).
Example: Energy is lost as heat during cellular respiration.
Importance: These laws govern energy flow and metabolism in living organisms.
Hydrophobic vs. Hydrophilic
Hydrophobic: "Water-fearing"; nonpolar molecules (e.g., lipids).
Hydrophilic: "Water-loving"; polar molecules.
Phospholipid Membrane:
Hydrophilic heads face water (outside and inside).
Hydrophobic tails face inward, away from water.
Properties of Water and Polarity
Water is polar: Oxygen has a partial negative charge, hydrogens are partially positive.
Hydrogen Bonds: Weak bonds between water molecules (H⁺ of one water molecule and O⁻ of another).
Solvation: Water dissolves polar substances because it can surround and interact with them.
Denaturation
Loss of protein structure and function due to:
Changes in pH, temperature, or substrate concentration.
Example: Cooking an egg denatures its proteins.
Enzymes
Definition: Proteins that act as biological catalysts to speed up chemical reactions.
How They Work: Lower activation energy by stabilizing the transition state.
Induced Fit: Active site changes shape slightly to fit the substrate.
Environmental Factors:
pH, temperature, and substrate concentration affect enzyme activity.
Inhibition:
Competitive: Inhibitor binds to the active site.
Noncompetitive: Inhibitor binds elsewhere, changing enzyme shape.
Cell Size and Surface Area-to-Volume Ratio
Why It Matters: As a cell grows, its volume increases faster than its surface area, leading to:
Decreased surface area-to-volume ratio.
Limits on material exchange (e.g., nutrients, waste) across the cell membrane.
Effect on Cell Size: Cells remain small to maintain a high surface area-to-volume ratio for efficient transport.
Cellular Organelles and Functions
1. Organelles Common to Both Prokaryotes and Eukaryotes:
Cell membrane: Regulates what enters/exits the cell.
Ribosomes: Protein synthesis.
2. Eukaryotic Organelles (Absent in Prokaryotes):
Nucleus: Stores DNA.
Mitochondria: ATP production (cellular respiration).
Chloroplasts (plants): Photosynthesis.
Endoplasmic Reticulum (ER):
Rough ER: Protein production (associated with ribosomes).
Smooth ER: Lipid synthesis, detoxification.
Golgi Apparatus: Modifies, sorts, and packages proteins.
Lysosomes: Break down waste (animal cells).
Vacuoles: Storage (large central vacuole in plants).
Cytoskeleton: Structure and transport.
3. Prokaryotic Structures:
No nucleus or membrane-bound organelles.
Nucleoid: Region with DNA.
Flagella: Movement.
4. Plant vs. Animal Cells:
Plant-Specific: Chloroplasts, central vacuole, cell wall.
Animal-Specific: Lysosomes, centrioles.
Endomembrane System
Definition: A network of organelles involved in protein and lipid synthesis, modification, and transport.
Components:
Rough ER: Protein synthesis.
Golgi Apparatus: Modifies and packages proteins.
Vesicles: Transport materials.
Lysosomes: Digestive enzymes (animal cells).
Protein Pathways
Secretory Protein:
Ribosomes → Rough ER → Transport Vesicle → Golgi Apparatus → Vesicle → Cell Membrane (exocytosis).
Cytosolic Protein:
Synthesized on free ribosomes → Remains in the cytoplasm.
Fluid Mosaic Model
Components: Phospholipids, proteins, cholesterol, carbohydrates.
Cholesterol: Stabilizes the membrane; maintains fluidity (prevents too much rigidity or fluidity).
Types of Transport
Passive Transport: No energy required.
Simple Diffusion: Movement of small, nonpolar molecules (e.g., O₂, CO₂).
Facilitated Diffusion: Movement via transport proteins (e.g., glucose, ions).
Osmosis: Diffusion of water across a semipermeable membrane.
Tonicity:
Hypotonic: Water enters; cells swell (plants become turgid; animals may burst).
Hypertonic: Water leaves; cells shrink (plasmolysis in plants, crenation in animals).
Isotonic: Equal water movement; cells remain the same size.
Active Transport: Requires energy (ATP).
Examples: Sodium-potassium pump, proton pump.
Bulk Transport:
Exocytosis: Materials exit the cell.
Endocytosis: Materials enter the cell (phagocytosis, pinocytosis, receptor-mediated endocytosis).
Cell Signaling
Ligands: Molecules that bind to receptors to trigger a response.
Steroid Hormones:
Hydrophobic; diffuse through membranes and bind intracellular receptors to activate transcription.
Protein Kinases: Enzymes that phosphorylate proteins (activate/inhibit).
cAMP: Secondary messenger that amplifies signals.
G Proteins: Transmit signals from receptors to target enzymes.
Coupled Reactions and ATP
Coupled Reactions: Energy-releasing reactions drive energy-requiring reactions.
ATP:
Structure: Adenine, ribose sugar, 3 phosphate groups.
Function: Energy is released by breaking the terminal phosphate bond.
Photosynthesis and Cellular Respiration
Photosynthesis Equation:
6CO2+6H2O+light→C6H12O6+6O2Cellular Respiration Equation:
C6H12O6+6O2→6CO2+6H2O+ATP
Fate of Oxygen: Oxygen is the final electron acceptor in the electron transport chain, forming water.
Biochemical Reactions
Light Reaction: Occurs in thylakoid membrane; produces ATP, NADPH, and O₂.
Calvin Cycle: Occurs in stroma; uses ATP, NADPH, and CO₂ to make G3P.
Glycolysis: Cytoplasm; glucose → 2 pyruvate, 2 ATP, 2 NADH.
Pyruvate Oxidation: Mitochondria; pyruvate → Acetyl-CoA, CO₂, NADH.
Krebs Cycle: Mitochondrial matrix; produces NADH, FADH₂, ATP, CO₂.
ETC: Inner mitochondrial membrane; generates ATP via oxidative phosphorylation.
Fermentation
Occurs without oxygen.
Types:
Lactic Acid: Pyruvate → Lactate (muscle cells).
Alcoholic: Pyruvate → Ethanol + CO₂ (yeast).
Photosynthesis Adaptations
C3 Plants: Standard Calvin cycle.
C4 Plants: Separate carbon fixation in mesophyll cells to reduce photorespiration (e.g., corn).
CAM Plants: Stomata open at night to fix CO₂ (e.g., cacti).
Cell Cycle
Phases: G1 → S → G2 → Mitosis → Cytokinesis.
Mitosis: Interphase, Prophase, Metaphase, Anaphase, Telophase.
Regulation:
Cyclins and CDKs: Proteins that regulate progression.
Checkpoints: Ensure proper division.
P53: Tumor suppressor protein.
Cancer: Uncontrolled cell division due to checkpoint failures.
Chi-Square Analysis
Used to compare observed vs. expected data.
Equation: X^2=∑(O−E)^2/E
O: Observed, E: Expected.
Compare X2X^2X2 value to critical value to determine significance.
Error Bars and Histograms
Error Bars: Represent variability or standard error in data.
HOW DO YOU READ ERROR BARS?????? THERE ARE THREE TYPES!!!!
Histograms: Show frequency distributions of data.