Biology Notes: Modules 1-3 (Brief)

Module 1: Introduction to Biology

  • Properties of life: Order; response to stimuli; reproduction; adaptation; growth & development; regulation; homeostasis; energy processing
  • Levels of organization (small → large): Molecule→Cell→Tissue→Organ→Organ system→Organism→Population→Community→Ecosystem→Biosphere\text{Molecule} \rightarrow \text{Cell} \rightarrow \text{Tissue} \rightarrow \text{Organ} \rightarrow \text{Organ system} \rightarrow \text{Organism} \rightarrow \text{Population} \rightarrow \text{Community} \rightarrow \text{Ecosystem} \rightarrow \text{Biosphere}
  • Three domains of life: Bacteria, Archaea, Eukarya
  • Taxonomy (largest → smallest): Domain → Kingdom → Phylum → Class → Order → Family → Genus → Species
  • Binomial nomenclature: Scientific name = Genus + species
  • Phylogenetic tree: Diagram showing evolutionary relationships
  • Observation (scientific method) → Information gathered with senses; Hypothesis → Proposed explanation; Prediction → Testable statement from hypothesis; Experiment → Controlled test; Conclusion → Support or reject hypothesis
  • Variables: Independent variable → The factor that is changed; Dependent variable → The factor that is measured; Control variable → Factors kept constant
  • Reasoning: Deductive reasoning → General → specific; Inductive reasoning → Specific → general

Module 2: Chemistry of Life

  • Matter → Anything that takes up space and has mass
  • Element → Substance that cannot be broken down
  • Atom → Smallest unit of an element
  • Subatomic particles → Protons (+, nucleus); Neutrons (0, nucleus); Electrons (−, orbitals)
  • Atomic number → #\text{protons}; Mass number → Protons + neutrons
  • Isotopes → Same element, different neutrons
  • Valence shell → Outermost electron shell; Valence electrons → Electrons in outer shell
  • Ionic bond → Transfer of electrons (cation +, anion -)
  • Covalent bond → Sharing electrons
  • Nonpolar covalent → Equal sharing; Polar covalent → Unequal sharing
  • Hydrogen bonds → Weak attraction between slightly + hydrogen and slightly − atom
  • Bond strength (strongest → weakest) → Covalent > Ionic > Hydrogen
  • Water is polar → Regions of partial + and − charges
  • Properties of water → Stabilizes temperature, excellent solvent, cohesive/adhesive
  • Cohesion → Water molecules stick to each other; Adhesion → Water molecules stick to other surfaces
  • pH scale → 0−140-14
  • Acid → pH<7pH < 7; Base → pH>7pH > 7; Neutral → pH=7pH = 7
  • Buffers → Maintain stable pH in organisms (e.g., CO₂ in blood)

Module 3: Biological Macromolecules

  • Organic molecules → Always contain carbon
  • Why carbon forms 4 bonds? → 4 valence electrons
  • Monomer → Small building block; Polymer → Chain of monomers
  • Dehydration reaction → Joins monomers into polymers (removes water)
  • Hydrolysis → Breaks polymers into monomers (adds water)
  • Carbohydrates
    • General formula → C(H<em>2O)</em>nC(H<em>2O)</em>n
    • Function → Energy, cell wall structure
    • Monosaccharide → 1 sugar (ex: glucose)
    • Disaccharide → 2 sugars via dehydration (ex: sucrose, maltose, lactose)
    • Polysaccharide → Long sugar chains
    • Starch → Energy storage in plants
    • Cellulose → Cell walls in plants
    • Glycogen → Energy storage in humans
    • Sugar suffix → -ose
  • Lipids → Nonpolar, hydrophobic
    • Functions → Long-term energy, insulation, hormones, membranes, waterproofing
    • Fat (triglyceride) → Glycerol + 3 fatty acids
    • Fatty acids → Saturated → Single bonds, straight, solid at room temp; Unsaturated → Double bonds, bent, liquid at room temp
    • Phospholipids → Cell membranes; Head = hydrophilic; Tail = hydrophobic
    • Steroids → Fused ring structures (cholesterol, hormones)
    • Waxes → Prevent water sticking to surfaces
  • Proteins → Monomer = Amino acid
    • Amino acid components → Amino group, carboxyl group, R group, hydrogen
    • Primary structure → Amino acid sequence
    • Secondary structure → α-helix or β-sheet (H bonds)
    • Tertiary structure → 3D folding (R group interactions)
    • Quaternary structure → Multiple polypeptides
    • Denaturation → Protein loses shape (heat, pH, salt)
    • Functions → Enzymes, structure, hormones, defense, transport
    • Enzymes → Speed up chemical reactions
    • Protein function depends on → Shape
  • Nucleic Acids
    • Monomer → Nucleotide = sugar + phosphate + base
    • DNA → Sugar = deoxyribose; Bases = A, T, C, G
    • RNA → Sugar = ribose; Bases = A, U, C, G
    • DNA function → Stores genetic information
    • RNA functions → mRNA, rRNA, tRNA
    • Base pairs (DNA) → A–T, C–G
    • Base pairs (RNA) → A–U, C–G