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Carbohydrates
Organic molecules (C, H, O in 1:2:1) used for quick energy, energy storage, and structure
Monosaccharide
Single sugar unit; building block of carbohydrates (ex: glucose)
Disaccharide
Two monosaccharides joined by a glycosidic linkage
Structural carbohydrates
Cellulose (plant cell walls; rigidity)
Chitin (fungi cell walls; protection)
Storage carbohydrates
Starch (plants; glucose storage)
Glycogen (animals; short
Proteins
Polymers of amino acids that function as enzymes, structure, transport, movement, and signaling
Amino acid
Protein monomer with amino group, carboxyl group, R group (determines properties)
Peptide bond
Covalent bond formed by dehydration synthesis between amino acids
Primary structure
Specific amino acid sequence (determines all higher structure)
Secondary structure
Alpha helices or beta sheets from hydrogen bonding in backbone
Tertiary structure
Overall 3D shape from R-group interactions (H-bonds, ionic, disulfide)
Quaternary structure
Multiple polypeptide chains forming one functional protein
Nucleic acids
Polymers that store, transmit, and express genetic information
Nucleotide
Phosphate + pentose sugar + nitrogenous base
Phosphodiester linkage
Covalent bond between nucleotides forming sugar-phosphate backbone
DNA vs RNA bases
DNA: thymine (T)
RNA: uracil (U)
DNA vs RNA sugar
DNA: deoxyribose
RNA: ribose
DNA vs RNA structure
DNA: double-stranded
RNA: single-stranded
DNA orientation
Antiparallel strands running 5′ → 3′ (direction of synthesis)
Lipids
Nonpolar molecules used for long-term energy, membranes, insulation, hormones
Fats
Glycerol + three fatty acids; energy storage
Saturated fatty acids
No double bonds; straight chains; solid at room temp
Unsaturated fatty acids
One or more double bonds; bent chains; liquid at room temp
Phospholipids
Amphipathic molecules forming cell membranes
Steroids
Four fused rings; function as hormones (ex: testosterone)
Water polarity
Unequal electron sharing allows hydrogen bonding
Cohesion
Water sticks to water (surface tension)
Adhesion
Water sticks to polar surfaces (capillary action)
Universal solvent
Dissolves ionic and polar substances
High specific heat
Buffers temperature changes in organisms
Ice density
Hydrogen bonds form lattice → ice floats
Nucleus
Stores DNA; site of transcription; assembles ribosomal subunits
Ribosomes
Translate mRNA into polypeptides
Rough ER
Synthesizes proteins for secretion or membranes
Smooth ER
Lipid synthesis; detoxification; Ca²⁺ storage
Golgi apparatus
Modifies proteins (ex: glycosylation), sorts, and ships them
Mitochondria
Produces ATP through aerobic respiration
Krebs cycle
Matrix; breaks acetyl-CoA into CO₂, NADH, FADH₂
Oxidative phosphorylation
Cristae; ETC builds proton gradient → ATP
Chloroplast
Converts light energy to chemical energy
Light reactions
Thylakoid; water split → O₂, ATP, NADPH
Calvin cycle
Stroma; CO₂ fixed into G3P using ATP/NADPH
Lysosome
Intracellular digestion; recycling; apoptosis
Vacuole
Storage; water balance; maintains turgor pressure
Surface area-to-volume ratio
Higher ratio allows faster diffusion of materials
Plasma membrane
Fluid mosaic of phospholipids, proteins, carbs, cholesterol
Passive transport
Moves substances down concentration gradient without ATP
Simple diffusion
Small, nonpolar molecules cross membrane directly
Facilitated diffusion
Polar molecules use transport proteins; no energy
Active transport
Uses ATP to move substances against gradient
Ion pumps
Maintain electrochemical gradients (Na⁺/K⁺, Ca²⁺)
Endocytosis
Cell engulfs material into vesicles
(phago = solids, pino = liquids, receptor-mediated = specific)
Exocytosis
Vesicles fuse with membrane to release contents
Osmosis
Water moves from high to low water potential
Hypertonic
Water exits cell → shrinkage
Hypotonic
Water enters cell → swelling/lysis
Isotonic
No net water movement
Gibbs free energy
Energy available to drive cellular processes
Exergonic reaction
Releases energy; spontaneous (ATP hydrolysis)
Endergonic reaction
Requires energy input (ATP synthesis)
Enzymes
Proteins that lower activation energy by stabilizing transition state
Competitive inhibitors
Block active site; resemble substrate
Noncompetitive inhibitors
Change enzyme shape; reduce activity
Denaturation
Loss of shape → loss of function
Glycolysis
Cytosol; glucose → 2 pyruvate + ATP + NADH
ETC
Cristae; electrons power proton pumps
Final electron acceptor
Oxygen (forms water)
Chemiosmosis
Proton flow through ATP synthase → ATP
Photosynthesis
Stores light energy as chemical energy
Light reactions
Light + H₂O → ATP + NADPH + O₂
Calvin cycle
CO₂ → G3P (sugar precursor)
Signal transduction
Reception → signal amplification → response
Steroid hormones
Diffuse through membrane; regulate gene expression
Protein hormones
Bind surface receptors; trigger cascades
Secondary messengers
Amplify signal inside cell (cAMP, Ca²⁺)
G₁
Growth; organelle duplication
S
DNA replication
G₂
Final growth and error checking
Mitosis
Nuclear division (PMAT)
Cytokinesis
Cytoplasm divides
Mitosis outcome
2 genetically identical diploid cells
Meiosis outcome
4 genetically unique haploid cells
Crossing over
Homologous chromosomes exchange DNA (Prophase I)
Independent assortment
Random alignment of homologs (Metaphase I)
Complete dominance
Dominant allele fully masks recessive
Codominance
Both alleles fully expressed
Incomplete dominance
Heterozygote shows intermediate phenotype
Replication
DNA → DNA
Helicase unwinds; primase primes; DNA polymerase builds 5′ → 3′
Transcription
DNA → mRNA
RNA polymerase reads template strand and builds mRNA 5′ → 3′
RNA processing
5′ cap protects; poly-A tail stabilizes; introns removed via splicing
Translation
mRNA → polypeptide
Ribosome reads codons; tRNA brings amino acids; peptide bonds form
Operons
Gene clusters regulated together
Repressible operon (Trp)
Normally ON
Substrate: tryptophan
Product effect: tryptophan activates repressor → operon OFF
Inducible operon (Lac)
Normally OFF
Substrate: lactose
Product effect: lactose inactivates repressor → operon ON
Silent mutation
Codon change; same amino acid
Missense mutation
Codon change; different amino acid
Nonsense mutation
Codon becomes STOP → shortened protein
Frameshift mutation
Insertion/deletion shifts reading frame → major protein disruption