AS

Comprehensive Biology 1 Study Guide (by Abdullah Sultan)

Biology Finals Study Guide

UNIT 1: BIOLOGICAL MACROMOLECULES

Functional Groups

Group

Structure

Properties

Hydroxyl (-OH)

-OH

Polar, forms hydrogen bonds, increases water solubility

Carboxyl (-COOH)

-COOH

Acidic, polar, can donate H⁺

Amino (-NH₂)

-NH₂

Basic, polar, can accept H⁺

Carbonyl (C=O)

C=O

Polar

Phosphate (-OPO₃²⁻)

-OPO₃²⁻

Negatively charged, transfers energy

Sulfhydryl (-SH)

-SH

Forms disulfide bridges

Methyl (-CH₃)

-CH₃

Nonpolar, hydrophobic

Macromolecules Overview

Macromolecule

Monomer

Examples

Functions

Carbohydrates

Monosaccharides

Glucose, fructose, starch, glycogen, cellulose

Energy storage, structural support

Proteins

Amino acids

Enzymes, collagen, keratin, insulin

Catalysis, structure, transport, signaling

Lipids

Fatty acids (not true monomers)

Triglycerides, phospholipids, waxes, cholesterol

Energy storage, cell membranes, insulation

Nucleic Acids

Nucleotides

DNA, RNA, ATP

Genetic information, energy transfer

Polymerization and Depolymerization

  • Dehydration Synthesis (Condensation): Monomers join, releasing water (H₂O)

    • Builds polymers (anabolic)

    • Requires energy

  • Hydrolysis: Polymers break down by adding water

    • Breaks down polymers (catabolic)

    • Releases energy

Carbohydrates

  • Formula: (CH₂O)ₙ - carbon, hydrogen, oxygen in 1:2:1 ratio

  • Monosaccharides: Simple sugars (glucose, fructose, galactose)

  • Disaccharides: Two monosaccharides (sucrose = glucose + fructose)

  • Polysaccharides: Many monosaccharides

    • Starch/Glycogen: Energy storage in plants/animals

    • Cellulose/Chitin: Structural components in plants/insects

Lipids

  • Hydrophobic molecules - insoluble in water

  • Triglycerides: 3 fatty acids + glycerol backbone

    • Saturated: No double bonds, solid at room temp

    • Unsaturated: Contains double bonds, liquid at room temp

  • Phospholipids: 2 fatty acids + phosphate group - form cell membranes

  • Steroids: 4 fused carbon rings (cholesterol)

  • Waxes: Long-chain fatty acids + alcohols

Nucleic Acids

  • Nucleotide structure: Sugar + phosphate + nitrogenous base

  • DNA: Deoxyribose sugar, double helix, A-T and G-C base pairs

  • RNA: Ribose sugar, single strand, A-U and G-C base pairs

  • Function: Genetic information storage and transfer

UNIT 2: PROTEINS & ENZYMES

Amino Acids

  • 20 different types with same backbone (NH₂-C-COOH) but different R groups

  • Classified by properties of R group:

    • Nonpolar/Hydrophobic: Alanine, valine, leucine, isoleucine, etc.

    • Polar/Hydrophilic: Serine, threonine, cysteine, etc.

    • Acidic: Aspartic acid, glutamic acid

    • Basic: Lysine, arginine, histidine

Protein Structure

  1. Primary: Amino acid sequence linked by peptide bonds

  2. Secondary: Regular patterns formed by hydrogen bonds

    • α-helix: Spiral structure

    • β-sheet: Pleated structure

  3. Tertiary: Overall 3D shape due to R group interactions

    • Hydrophobic interactions

    • Ionic bonds

    • Hydrogen bonds

    • Disulfide bridges (between cysteine residues)

  4. Quaternary: Multiple polypeptide chains together

Protein Denaturation

  • Loss of structure and function due to:

    • Temperature changes

    • pH changes

    • Salt concentration changes

  • Primary structure remains intact

  • Higher levels of structure are disrupted

Enzymes

  • Biological catalysts that speed up reactions

  • Lower activation energy required for reactions

  • Substrate specificity: Active site binds only specific substrates

  • Enzyme-substrate complex: Temporary structure during catalysis

  • Induced fit model: Active site shape adjusts to fit substrate

Enzyme Kinetics

  • Factors affecting enzyme rate:

    1. Enzyme concentration: Linear relationship until substrate limiting

    2. Substrate concentration: Hyperbolic curve leading to saturation

    3. Temperature: Rate increases until optimum, then decreases (denaturation)

    4. pH: Each enzyme has optimal pH range

    5. Inhibitors: Substances that reduce enzyme activity

Enzyme Inhibition

  • Competitive inhibition: Inhibitor resembles substrate, competes for active site

  • Non-competitive inhibition: Inhibitor binds elsewhere, changes enzyme shape

UNIT 3: DNA/GENE EXPRESSION & REGULATION

DNA Structure

  • Double helix of two antiparallel strands

  • Nucleotide: Deoxyribose sugar + phosphate + nitrogenous base (A, T, G, C)

  • Base pairing: A-T (2 hydrogen bonds), G-C (3 hydrogen bonds)

  • Sugar-phosphate backbone: Alternating sugar and phosphate groups

  • Chargaff's rule: A=T and G=C

DNA Packaging

  • DNA wound around histones to form nucleosomes

  • Nucleosomes coil into chromatin fibers

  • Chromatin condenses into chromosomes during cell division

  • Humans have 23 pairs of chromosomes

The Central Dogma

  • DNA → RNA → Protein

  • Transcription: DNA → RNA

  • Translation: RNA → Protein

Transcription

  1. Initiation: RNA polymerase binds to promoter with help of transcription factors

  2. Elongation: RNA polymerase synthesizes RNA (using DNA template strand)

  3. Termination: RNA polymerase reaches termination sequence and detaches

RNA Processing (Eukaryotes)

  • 5' cap and 3' poly-A tail added

  • Introns (non-coding regions) removed

  • Exons (coding regions) spliced together

  • Alternative splicing: Different arrangements of exons create different proteins

Translation

  1. Initiation: Ribosome assembles at start codon (AUG)

  2. Elongation: tRNAs bring amino acids; peptide bonds form

  3. Termination: Stop codon (UAA, UAG, UGA) reached, polypeptide released

The Genetic Code

  • Codon: 3 nucleotides code for 1 amino acid

  • Degenerate: Multiple codons can code for same amino acid

  • Universal: Same in most organisms

Gene Regulation in Prokaryotes: Operons

  • Operon: Cluster of genes with related functions controlled together

  • Lac Operon: Activated when lactose present, glucose absent

    • Repressor: Binds to operator when lactose absent

    • Inducer: Lactose binds to repressor, prevents operator binding

  • Trp Operon: Repressed when tryptophan present

    • Repressor: Inactive until it binds tryptophan

    • Co-repressor: Tryptophan activates repressor

Genetic Engineering

  • Recombinant DNA: DNA from different sources combined

  • Plasmids: Small circular DNA molecules in bacteria

    • Origin of replication: Allows plasmid replication

    • Selectable marker: Often antibiotic resistance gene

    • Cloning site: Where new genes can be inserted

  • Bacterial transformation: Introduction of foreign DNA into bacteria

Mutations

  • Point mutations: Change in single nucleotide

    • Silent: No change in amino acid

    • Missense: Different amino acid coded

    • Nonsense: Creates premature stop codon

  • Frameshift mutations: Insertion or deletion shifts reading frame

    • Often more severe than point mutations

UNIT 4: PHOTOSYNTHESIS & CELLULAR RESPIRATION

Photosynthesis Overview

  • Equation: 6CO₂ + 6H₂O + light energy → C₆H₁₂O₆ + 6O₂

  • Location: Chloroplasts in plant cells

  • Two main stages:

    1. Light-dependent reactions

    2. Calvin cycle (light-independent reactions)

Light-Dependent Reactions

  • Location: Thylakoid membrane

  • Process:

    1. Light energy absorbed by chlorophyll

    2. Water molecules split (photolysis): 2H₂O → 4H⁺ + 4e⁻ + O₂

    3. Electrons move through electron transport chain

    4. ATP produced by chemiosmosis (ATP synthase)

    5. NADP⁺ reduced to NADPH

  • Products: ATP, NADPH, O₂

Calvin Cycle (Light-Independent Reactions)

  • Location: Stroma

  • Process:

    1. Carbon fixation: CO₂ combines with RuBP (catalyzed by Rubisco)

    2. Reduction: ATP and NADPH from light reactions used to form G3P

    3. Regeneration of RuBP using ATP

  • Products: Glucose, other organic compounds

Cellular Respiration Overview

  • Equation: C₆H₁₂O₆ + 6O₂ → 6CO₂ + 6H₂O + ATP

  • Stages:

    1. Glycolysis

    2. Pyruvate processing

    3. Krebs cycle (Citric Acid Cycle)

    4. Electron Transport Chain & Oxidative Phosphorylation

Glycolysis

  • Location: Cytoplasm

  • Process: Glucose (6C) split into 2 pyruvate (3C) molecules

  • Net products (per glucose):

    • 2 ATP

    • 2 NADH

    • 2 Pyruvate

  • Anaerobic: No oxygen required

Pyruvate Processing

  • Location: Mitochondrial matrix

  • Process: Pyruvate (3C) → Acetyl-CoA (2C) + CO₂

  • Products (per pyruvate):

    • 1 NADH

    • 1 CO₂

    • 1 Acetyl-CoA

Krebs Cycle

  • Location: Mitochondrial matrix

  • Process: Acetyl-CoA enters cycle, regenerates starting compound

  • Products (per acetyl-CoA):

    • 3 NADH

    • 1 FADH₂

    • 1 ATP (GTP)

    • 2 CO₂

Electron Transport Chain & Oxidative Phosphorylation

  • Location: Inner mitochondrial membrane

  • Process: Electrons from NADH and FADH₂ move through proteins

    • Energy used to pump H⁺ into intermembrane space

    • H⁺ gradient powers ATP synthase (chemiosmosis)

  • Final electron acceptor: O₂, forming H₂O

  • Products: ~34 ATP (total from all stages)

ATP Yield Summary

  • Glycolysis: 2 ATP + 2 NADH (→ ~4 ATP) = ~6 ATP

  • Pyruvate processing: 2 NADH (→ ~6 ATP)

  • Krebs cycle: 2 ATP + 6 NADH (→ ~18 ATP) + 2 FADH₂ (→ ~4 ATP) = ~24 ATP

  • Total: ~36 ATP per glucose molecule

Environmental Connections

  • Photosynthesis and CO₂ levels:

    • Plants absorb CO₂ during photosynthesis

    • Rising atmospheric CO₂ leads to ocean acidification

    • Ocean pH decreases as more CO₂ dissolves in water

  • Cellular respiration and metabolism:

    • Tissues with high energy needs (muscle, nerve) have more mitochondria

    • Other energy sources: Lipids and proteins can enter respiratory pathways