Observation: Initial step; involves noticing phenomena and gathering information.
Hypothesis: A testable explanation for the observed phenomena; an educated guess.
Experimental design:
Control: A group that does not receive the experimental treatment; used as a baseline for comparison. Contains everything EXCEPT the experimental variable.
Experimental variable(s): The factor being tested or changed in the experiment. Controlled and manipulated by the researcher.
Results:
Statistics: Mathematical analyses of the data collected to determine significance.
Graphs: Visual representations of data to show trends and relationships.
Discussion: Interpretation of the results in the context of the hypothesis. Comparison with existing knowledge and literature.
Conclusion:
Hypothesis is true/supported/confirmed: Indicates that the data supports the initial hypothesis.
Hypothesis is not correct: Indicates that the data does not support the initial hypothesis, requiring a revised hypothesis (back to the drawing board!)
Bias: Scientific prejudice. Systematic errors in the experimental design or interpretation of data.
Scientific fraud: Doctoring the data. Intentional manipulation or falsification of research data.
Organic Molecules:
Contain Carbon (C) and Hydrogen (H). Fundamental building blocks of living organisms.
Covalent bonding: Involves sharing of valence or outer-shell electrons, following the octet rule to achieve stability.
Inorganic Molecules:
Examples: NH3, H2O, CO2, HCl, H3PO4, H2SO_4
Bonding:
Covalent Bonding: Sharing of electrons between atoms.
Ionic Bonding: Attraction between positive and negative ions, resulting in electron transfer.
Non-bonding Associations:
Hydrogen bonding: Between H and an electronegative element (e.g., water). Weak but crucial for stabilizing biological molecules.
Dipole-dipole interaction: Molecule has positive and negative ends, leading to electrostatic attraction.
Van der Waals: Weaker interactions due to temporary fluctuations in electron distribution.
Examples: -CH3 (methyl), -OH (hydroxyl), O=C- (carbonyl), -NH2 (amino), -PO_4H (phosphate), -COOH (carboxyl)
Dehydration: Removing water to make a bond (anabolic/synthesis of larger molecules). Results in the formation of a covalent bond.
Hydrolysis: Breaking a bond with water (polymer + H_2O -> monomers; catabolic -> breakdown of larger molecules). Reverses dehydration.
Monomer: Glucose (monosaccharide). Simple sugar; primary energy source for cells.
Polysaccharides: Glycogen (in animals), starch (in plants). Polymers of glucose; storage forms of energy.
Function: Storing energy, structure (cellulose, chitin). Structural components in cell walls (cellulose) and exoskeletons (chitin).
Characteristics: Do not dissolve in water. Hydrophobic nature.
Components: Fatty acids and glycerol. Building blocks of lipids.
Functions: Stored form of energy, phospholipids (membrane), cholesterol, steroids (hormones). Diverse functions in energy storage, membrane structure, and cell signaling.
Structure:
Hydrocarbon tail (non-polar) -> Hydrophobic: Repels water.
Polar head (contains O, N, P) -> Hydrophilic: Attracts water.
Monomers: 20 amino acids. Building blocks of proteins; each with a unique side chain.
Polymers:
Four levels of structure:
Primary: Specific amino acid sequence. Linear chain of amino acids.
Secondary: Alpha helix, beta-pleated sheet. Local folding patterns stabilized by hydrogen bonds.
Tertiary: 3-D shape/folding into a functional polypeptide. Overall shape determined by various interactions.
Quaternary: Two or more polypeptides in association (collagen, hemoglobin). Multiple polypeptide subunits combine to form a functional protein.
Function: Enzyme, support, actin, myosin, antibody. Diverse roles including catalyzing reactions, structural support, muscle contraction, and immune defense.
DNA: Double-stranded, deoxyribose sugar, ATCG. Contains blueprints to make polypeptides. Stores genetic information.
RNA: Single-stranded, ribose sugar, AUCG. Types: mRNA, tRNA (carries an amino acid), rRNA (made in the nucleolus). Involved in protein synthesis and gene regulation.
Saturated Lipids: All carbon molecules with single bonds; animal origin. Solid at room temperature because their straight structure allows them to pack tightly.
Unsaturated Lipids: Carbons bonded with double/triple bonds; plant origin (olive, sunflower). Liquid at room temperature due to kinks in the fatty acid chains.
Breakdown of polypeptide/protein structure; likely non-functional. Disrupts the native conformation of the protein.
Causes: Heat, light, salt, acid, base (e.g., egg white). Disrupts the bonds that maintain secondary and tertiary structures.
Golgi apparatus: Packaging/deployment, vesicle formation (secretory and transitory vesicles). Modifies, sorts, and packages proteins and lipids.
Nucleus: Double membrane, nuclear pores, contains genetic material. Control center of the cell; contains DNA.
Rough Endoplasmic Reticulum (RER): Protein synthesis. Ribosomes attached for synthesizing and modifying proteins.
Smooth Endoplasmic Reticulum (SER): Lipid synthesis. Involved in lipid and steroid hormone synthesis; detoxification.
Ribosomes: Site of protein synthesis (70% protein, 30% rRNA). Translate mRNA into proteins.
Mitochondrion: Double-membraned, produces energy. Powerhouse of the cell; site of cellular respiration.
Lysosomes: Digestive enzymes/housekeepers. Break down cellular waste and debris.
Peroxisomes: Break down peroxides. Detoxify harmful substances.
Chloroplasts: Double-membraned, photosynthesis; grana (thylakoid membranes), stroma, lamellae. Site of photosynthesis in plant cells.
Cytoskeleton: Filaments: actin (microfilaments), intermediate, microtubules. Provides structural support, cell shape, and movement.
Centrioles: 9 triplets microtubule arrangement + 0. Involved in cell division.
Flagellum: 9 doublets + 2; mobility. Long, whip-like structure for cell movement.
Cilia: 9 doublets + 2; mobility (paramecium), stereocilia. Short, hair-like structures for movement or sensory functions.
Basal body: 9 + 0. Anchors flagella and cilia.
Cell wall: Plants. Provides rigid support and protection.
Phospholipid bilayer with embedded proteins.
Fluid: Phospholipid bilayer. Allows lateral movement of lipids and proteins.
Mosaic: Embedded proteins. Proteins are dispersed throughout the lipid bilayer.
Hydrophilic portion: Likes water. Polar heads of phospholipids.
Hydrophobic portion: Fears water. Non-polar tails of phospholipids.
Semi-permeable membrane/selectivity. Controls the movement of substances in and out of the cell.
Plasma membrane = cytomembrane = cytolemma. Outer boundary of the cell.
Channel: Facilitates transport. Forms a pore for ions or molecules to pass through.
Cell recognition: Histocompatibility. Identifies cells as self or non-self.
Carrier: Facilitates transport. Binds to specific molecules and transports them across the membrane.
Receptor: Combines with molecules based on shape, size. Triggers cellular responses upon binding.
Enzymes: ATP synthetase. Catalyzes reactions at the membrane surface.
Signal transduction. Transmits external signals into the cell.
Sodium-potassium pump: Active transport. Maintains ion gradients across the membrane.
Solvent: Liquid that dissolves a solute. Typically water in biological systems.
Solute: Substance dissolved by the solvent. E.g., Salt or sugar.
Solution: Homogeneous mixture of solvent and solute. Uniform composition throughout.
Isotonic Solution: Equilibrium; no overt change in cell volume. Solute concentration is the same inside and outside the cell.
Hypotonic Solution: Less salt outside the cell; cell swells, may lyse. Water enters the cell, causing it to swell.
Hypertonic Solution: More salt outside the cell; cell releases water, shrivels, may undergo apoptosis (programmed cell death). Water leaves the cell, causing it to shrink.
Dialysis membrane: Size constraints determine what passes through. Allows separation of molecules based on size.
Active process: Needs energy (ATP); e.g., sodium-potassium pump. Moves substances against their concentration gradient.
Passive process: No energy expended:
Diffusion: High to low concentration. Movement of molecules from an area of high concentration to low concentration.
Facilitated transport: Across membrane. Requires carrier proteins or channels.
Osmosis: Diffusion of water. Movement of water across a semi-permeable membrane.
Exocytosis: Large molecules secreted via secretory vesicles. Releases substances from the cell.
Endocytosis: Small ions/molecules taken in via vesicle formation:
Pinocytosis: Cell drinking. Uptake of small droplets of fluid.
Phagocytosis: Cell eating. Uptake of large particles or cells.
Diffusion: Movement from high to low concentrations (gradient). Driven by the concentration gradient.
Osmosis: Movement of water from high to low water concentration. Water moves to equalize solute concentrations.
Gap: Flow of ions. Allows direct communication between cells.
Anchor/Intermediate: Tissue formation. Provides mechanical stability.
Tight Junction: Prevent leakage. Seals cells together to prevent passage of molecules.
Plants: Plasmodesmata (channels). Allows transport and communication between plant cells.
Catabolism: Break down (digestive processes). Releases energy.
Anabolism: Synthesis. Requires energy.
Substrate: Reactant/metabolite that becomes a product: S + E -> E-S complex -> P + E. The substance upon which an enzyme acts.
Enzyme: Protein catalyst; lock and key theory. Speeds up biochemical reactions.
Active Site: Where substrate binds and is converted to product.
Competitive inhibition: Chemical resembles substrate, binds to active site. Blocks substrate binding.
Non-competitive inhibition: Chemical binds elsewhere (allo), changes enzyme shape; feedback inhibition (A -> B -> C -> D -> E). Alters enzyme conformation, reducing activity.
Coenzyme: Organic molecules. Assists enzyme function.
Cofactors: Ions and coenzymes. Non-protein components that help enzymes.
First law: Cannot create or destroy energy; total energy is constant; law of conservation of energy. Energy can be converted from one form to another.
Second law: Energy transformation is not 100% efficient. Some energy is lost as heat, increasing entropy.
Oxidation: Lose electrons (lose H ion): NADH -> NAD^+ + 2e- + H^+. Loss of electrons or increase in oxidation state.
Reduction: Gain electrons (gain H ion). Gain of electrons or decrease in oxidation state.
Exergonic: Release of energy (-ΔG -> spontaneous). Reactions release free energy.
Endergonic: Need energy (+ΔG -> non-spontaneous). Reactions require an input of energy.
Exothermic: Release heat (-ΔH). Reactions release heat.
Endothermic: Require heat (+ΔH, ENTHALPY). Reactions absorb heat.
Factors affecting: Temperature (T), pH, [S] (substrate concentration), heavy metals (inhibit). Influences enzyme activity and reaction rates.
Optimal T, optimal pH, optimal [S]. Bell-shaped curve. Enzymes have specific conditions for maximal activity.
Structure: Adenine, sugar, 3 phosphates. Energy currency of the cell.
Function: Provides energy. Powers cellular processes.
Coupled reactions: Cycles, exchange of electrons/energy. Energy from exergonic reactions drives endergonic reactions.
Fixing carbon: Light reactions (PSI: make NADPH, ATP; PSII: make ATP) and dark reactions (Calvin Cycle). Conversion of light energy into chemical energy.
CO_2 ----> make sugar!!! Synthesis of glucose from carbon dioxide and water.
Components: Water, electrons, sunlight, chlorophyll, NADP^+, hydrogen ions, CO2, O2, PGAL, RuBP, glucose. Key players in photosynthesis.
Light dependent: PSI and PSII. Converts light energy into chemical energy (ATP and NADPH).
Light independent: Calvin cycle – formation of PGAL (ATP and NADPH used) in stroma. Uses ATP and NADPH to fix carbon and produce sugars.
Aerobic respiration: Oxygen IS involved. Breakdown of glucose to produce ATP with oxygen.
Anaerobic respiration: Oxygen NOT involved (e.g., glycolysis). Breakdown of glucose without oxygen.
Fermentation: Lactic acid, ethanol. Produces ATP in the absence of oxygen.
Glycolysis: 2ATP and 2NADH (in cellular cytoplasm). Breakdown of glucose into pyruvate.
Krebs Cycle (TCA cycle): 2ATP, 6NADH, 2 FADH_2 (in matrix of mitochondria). Oxidizes acetyl-CoA to produce energy carriers.
Electron Transport: 34 ATP (cytochromes in inner mitochondrial membrane). Uses energy carriers to produce ATP.
Fats and proteins: Feed into glycolytic pathways. Can be used as alternative energy sources.
Asexual reproduction: Parent cell into two genetically identical daughter cells. Produces identical copies of cells.
Somatic cells: Growth of multicellular organism. Non-reproductive cells.
Human somatic cells: 46 chromosomes; daughter cells also have 46 chromosomes, diploid to diploid. Maintains chromosome number.
Cell Cycle
Interphase (Go): Chromosomes not visible. Cell grows and prepares for division.
Prophase: Nuclear envelope breaks down, see condensed chromatin (chromosomes). Chromosomes become visible.
Metaphase: Chromosomes line up. Chromosomes align at the metaphase plate.
Anaphase: Chromosomes move across the cell. Sister chromatids separate and move to opposite poles.
Telophase: Formation of nuclear envelopes, cleavage furrow (animal cell)/cell plate (plant cell) forming; followed by cytokinesis. Cell divides into two daughter cells.
Sexual reproduction: Gametes/diploid to haploid. Produces genetically diverse gametes.
Meiosis I: Reduction division, diploid->haploid; Prophase I: tetrad formation, recombination possible. Homologous chromosomes separate.
Meiosis II: Similar to mitosis (haploid to haploid). Sister chromatids separate.
Oogonia (diploid) -> primary oocytes (diploid, 46) ->MI-> secondary oocyte (haploid, 23)->MII-> ovum (haploid, 23) + 3 polar bodies…conservation of the cytoplasm in the final egg
Spermatogonia (diploid, 46) -> primary spermatocytes(diploid, 46)-> MI->secondary spermatocytes (haploid, 23) ->MII ->spermatids (haploid, 23) -> mature sperm cells (head, neck and flagella) (metamorphosis)
Homologous chromosomes form the tetrad (synapsis). Pairing of homologous chromosomes.
Recombination is possible -> genetic variability. Exchange of genetic material between homologous chromosomes.
Gamete (mature egg and mature sperm have 23 chromosomes )
Somatic Cells (46 chromosomes in humans)
Fertilized egg.
Zygote will start to reproduce via MITOSIS =====
Allele: Form of a gene: dominant allele -> uppercase letter; recessive allele -> lowercase letter
Gene: Carries the code to form a polypeptide.
Locus: Location of the gene/allele (on the chromosome).
Follow Mendel’s Laws:
Law of Probability (0.5).
Law of Independent assortment (alleles randomly sorted in formation of gametes).
Law of Segregation (alleles separate upon formation of the gametes).
Monohybrid (1 trait) versus Dihybrid (2 traits)
Dominant allele: Always seen in the majority of the population; only need one dominant allele to exhibit the dominant phenotype
Recessive allele: Seen less in the population; need both recessive alleles to exhibit the recessive phenotype [Phenotype: physical expression; Genotype: genetic makeup]
Homozygous dominant (DD), heterozygous (Dd) – considered a carrier, homozygous recessive (dd)
Mating DD with dd - > All phenotypes with dominant trait (Dd); DD x dd
Mate Dd with Dd -> 3:1 ratio of dom to rec (Phenotypic ratio) versus genotypic of 1:2:1 Dd x Dd
Use Punnett square for a one-trait and a two-trait cross
Two Trait (DiHybrid) Cross:
Parental AABB x aabb
F1 AaBb x AaBb
F2 : Phenotypic ratio: 9:3:3:1
9 AB : 3 Abb: 3 aaB : 1 aabb
AaBb -> gametes will be: AB, Ab, aB, ab
Pink Flower: incomplete dominance (another example: sickle cell trait); Recessive allele is not as masked, and starts to be expressed
Codominance: both alleles are expressed (type AB blood).
Polygenic Inheritance (think skin types) (think the sisters) [AaBBcc] (2 or more genes -> 1 trait)
Pleiotropy (1 gene –Many traits) – King George III. Sickle cell anemia
Environment (temperature and sex; habitat)
Separation of the chromosomes was not perfect
May occur in Meiosis I or Meiosis II
2n-1 (monosomy – Turner’s Syndrome), 2n+1 (trisomy – Down’s Syndrome)
* Deletion – chromosome gets shorter
* Translocation – two different chromosomes exchange part of their structure
* Replication – chromosome gets longer
* Inversion – flip of a segment of chromosome (180 degree) resulting in a different arrangement of the genes
* Formation of Rings
Gene Linkage (thank you Dr. Thomas H. Morgan):
Will be observed in phenotypic ratios of the offspring that DOES NOT FOLLOW THE MENDELIAN 9:3:3:1 ratio
Tightly linked -> distance between the alleles on the chromosome-> short
Loosely linked -> distance between the alleles on the chromosome -> longer
Mapping -> Frequencies of the phenotypes correlated to mapping distance
color blindness in males, hemophilia (Queen Victoria), MD
X^HX^h x X^HY -> X^HX^H, X^HX^h, X^HY, X^hY
Structure of dna (Deoxyribose sugar, phosphate – sugar phosphate backbone, ATCG); direction ( strand pairing with 5’-----3’)
Complementary base pairing: A with T, C with G Purine (2 rings) (A, G) hydrogen bonding with a pyrimidine (1 ring) (T, C)
DNA and RNA replication: initiation, elongation, termination
DNA replication is semi-conservative
Triplet Codon, Triplet anti-code (transfer RNA); codon codes for an amino acid
Genetic code – 64 possible combinations (4^3): redundant, non-ambiguous, universal, start and stop
Transcription occurs in the nucleus (eukaryotic organism) Primary mRna -> CAP AND TAIL ->SPLICEOSOMES (cut Introns)->mature mRNA (ALL EXONS)
Translation occurs in the cytoplasm (eukaryotic – endoplasmic reticulum, mitochondria, prokaryotic – cytoplasmic ribosomes/polyribosomes): mRNA, tRNA, rRNA
Diagram of Protein Synthesis
Parent DNA strand 3’-AAA-CGC-ATA-GAT-ACA-5’
Other parent strand for DNA 5’-TTT-GCG-TAT-CTA-TGT-3’
mRna 3’-AAA-CGC-AUA-GAU-ACA-5’
tRNA UUU GCG UAU CUA UGU (anticodon)
polypeptide Lys-Arg-Ile-Asp-Thr (from the mRNA)
DNA Synthesis -> leading strand and the lagging strand (Okazaki fragments -> DNA Ligase)
Helicase, DNA Polymerase, RNA primer, DNA Ligase
Transformation – involves introduction of foreign DNA, such the receiving organism is a recombinant and a transgenic organism
How to introduce foreign DNA into a plasmid or into viral DNA to give recombinant DNA
Gene therapy: in vivo and ex vivo
Darwin and the Five Assumptions for Natural Selection
Supportive Evidence: Fossils, Biogeography
Homologous structures
Analogous structures
Hardy-Weinberg Statistics – 1-mutations, 2-Gene Flow (migration – snake example), 3-Non-random mating, 4-genetic drift (founder’s effect, bottleneck), 5-Natural Selection (reproductive fitness)
Industrial melanism (white moth v black moth:
white dominant
black recessive;
but when trees turned dark -> population shift -> more black moths survived than white moths; as soon as pollution was abated, then shift back to more white moths over black moths)
formation of a species
Natural Selection:
1) Stabilizing -
2-Disruptive -
3-Directional
Allopatric (geographical) speciation
Sympatric (ecological) speciation
Origin of Life – Oparin’s Hypothesis, Miller & Urey experiment, protocells
Abiotic synthesis
Age of earth: 4.5 Billion years
Domain-> Kingdom -> Phylum -> Class -> Order -> Family -> Genus -> Species
Biomes: desert, tundra, grasslands (prairie and savanna), scrubland, taiga (Coniferous Forest), temperate (Deciduous Forest), Tropical Rain Forest
-
Here are the definitions of in vivo and ex vivo gene therapy:
In vivo: Gene therapy where genetic material is transferred directly into cells within the body.
Ex vivo: Gene therapy involving modification of cells outside the body before transplanting them back in.