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Bio Yr 12 Mock

The document provides an overview of microscopy techniques, cell structures, biological molecules, biochemical tests, nucleotides and nucleic acids, enzymes, biological membranes, and cell division. It details various microscopy methods, the functions of eukaryotic and prokaryotic cells, the composition of biological molecules, and the mechanisms of enzyme activity. Additionally, it covers the processes of cell division, including mitosis and meiosis, and the organization of cells into tissues and organs.

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0% found this document useful (0 votes)
7 views8 pages

Bio Yr 12 Mock

The document provides an overview of microscopy techniques, cell structures, biological molecules, biochemical tests, nucleotides and nucleic acids, enzymes, biological membranes, and cell division. It details various microscopy methods, the functions of eukaryotic and prokaryotic cells, the composition of biological molecules, and the mechanisms of enzyme activity. Additionally, it covers the processes of cell division, including mitosis and meiosis, and the organization of cells into tissues and organs.

Uploaded by

esha02219
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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1.

Microscopy 00:34

●​ Resolution is the minimum distance at which two objects can be distinguished as


separate. 01:41
●​ Magnification is how many times larger the image appears compared to the actual object.
02:03
●​ Light (Optical) Microscopes: 00:40
○​ Poor resolution due to the wavelength of light.
○​ Can view living samples and produce color images.
●​ Transmission Electron Microscopes (TEM): 01:03
○​ High magnification and resolution.
○​ Electrons pass through the specimen, creating a 2D image of internal structures.
○​ Samples must be very thin and in a vacuum.
●​ Scanning Electron Microscopes (SEM): 01:10
○​ Electrons bounce off the surface, creating a 3D image of the surface.
○​ Samples are coated and placed in a vacuum.
●​ Laser Scanning Confocal Microscopes: 01:24
○​ High resolution and 3D imaging using laser light.
●​ Slide Preparation Techniques: 02:09
○​ Dry Mount: Thin slices or whole specimens viewed with a cover slip.
○​ Wet Mount: Specimens in water or stain, covered with a cover slip.
○​ Squash Slide: Wet mount squashed to create a thin layer of cells.
○​ Smear Slide: Sample smeared across the slide for viewing (e.g., blood cells).
●​ Eyepiece Graticule Calibration: 03:55
○​ An eyepiece graticule is a scale in the microscope eyepiece used to measure
objects.
○​ A stage micrometer (a slide with a ruler) is used to calibrate the eyepiece
graticule at different magnifications.
○​ Each division on the stage micrometer is typically 10 micrometers.
○​ Calibration involves aligning the eyepiece graticule and stage micrometer scales
and calculating the value of one eyepiece graticule division.
●​ Magnification Calculation: 06:34
○​ Magnification = Image Size / Real Object Size
○​ Unit conversions (mm to μm) are often required (multiply mm by 1000 to get μm).
●​ Staining Techniques: 07:13
○​ Staining enhances visibility of cell components.
○​ Differential staining uses multiple stains to color different parts of the cell.
○​ Examples: Crystal violet, methylene blue (positive stains), Nigrosin, Congo red
(negative stains).
●​ Scientific Drawings: 08:18
○​ Use pencil, include a title, state magnification, label key features, annotate cell
components, use solid lines (no shading), and horizontal label lines.
○​ Aim is to show size, location, and proportion.2. Cell Structure 12:50
●​ Eukaryotic Cells: 13:02
○​ Contain membrane-bound organelles.
○​ Examples: animal, plant, and fungal cells.
○​ Key organelles and their functions:
■​ Nucleus: 13:21 Contains DNA, site of replication and transcription.
■​ Flagella: 14:15 Mobility (not in all eukaryotic cells).
■​ Cilia: 14:36 Hair-like projections for movement or sensory functions.
■​ Centrioles: 15:04 Involved in spindle fiber formation during cell division.
■​ Cytoskeleton: 15:34 Provides mechanical strength and support.
■​ Endoplasmic Reticulum (ER): 16:09
■​ Rough ER: Protein synthesis (has ribosomes).
■​ Smooth ER: Lipid and carbohydrate synthesis.
■​ Golgi Apparatus: 16:50 Modifies and packages proteins and lipids.
■​ Lysosomes: 17:52 Contain digestive enzymes for breaking down
materials.
■​ Mitochondria: 18:38 Site of aerobic respiration and ATP production.
■​ Ribosomes: 19:21 Protein synthesis (80S in eukaryotes).
■​ Chloroplasts: 20:02 (Plant cells) Site of photosynthesis.
■​ Cell Wall: 20:33 (Plant and fungal cells) Provides structural support.
■​ Plasma Membrane: 21:03 Controls what enters and exits the cell.
●​ Protein Production and Secretion: 21:47
○​ Polypeptide chains are synthesized on the rough ER (ribosomes).
○​ They move to the Golgi apparatus for modification and packaging into vesicles.
○​ Vesicles transport proteins to the cell surface membrane for exocytosis.
●​ Prokaryotic Cells: 22:52
○​ Smaller than eukaryotic cells.
○​ Lack membrane-bound organelles.
○​ Have 70S ribosomes.
○​ DNA is circular and free in the cytoplasm (no nucleus).
○​ Cell wall made of peptidoglycan.
○​ May have plasmids, a capsule, and flagella.

3. Biological Molecules 25:41

●​ Contain carbon.
●​ Carbohydrates, lipids, proteins, and nucleic acids.
●​ Ions: 26:01 Important roles (e.g., calcium, sodium, potassium, chloride, phosphate).
●​ Water: 26:50
○​ Polar molecule due to uneven charge distribution.
○​ Forms hydrogen bonds.
○​ Important solvent, transport medium, coolant (high specific heat capacity and
latent heat of vaporization), and provides habitats.
●​ Monomers and Polymers: 32:18
○​ Monomers are small units that bind together to form polymers.
○​ Examples:
■​ Glucose (monomer) forms starch, cellulose, and glycogen (polymers).
■​ Amino acids (monomer) form proteins (polymer).
■​ Nucleotides (monomer) form DNA and RNA (polymers).
●​ Carbohydrates: 33:08
○​ Contain carbon, hydrogen, and oxygen.
○​ Monosaccharides: Single sugar units (glucose, fructose, galactose, ribose).
○​ Disaccharides: Two sugar units joined by a glycosidic bond (sucrose, maltose,
lactose).
○​ Polysaccharides: Many sugar units (starch, cellulose, glycogen).
○​ Condensation Reaction: 37:41 Joins two molecules together by removing a water
molecule.
○​ Hydrolysis Reaction: 37:53 Splits a molecule by adding a water molecule.
○​ Starch: 39:35 (Plants) Storage of glucose (amylose and amylopectin).
○​ Cellulose: 41:44 (Plants) Structural support (beta glucose).
○​ Glycogen: 42:40 (Animals) Storage of glucose.
●​ Lipids: 43:34
○​ Non-polar, insoluble in water.
○​ Made of fatty acids and glycerol.
○​ Triglycerides: 44:05 Three fatty acids attached to glycerol (energy storage).
○​ Phospholipids: 44:05 Two fatty acids and a phosphate group attached to glycerol
(cell membranes).
○​ Saturated Fatty Acids: 45:23 Have only single bonds.
○​ Unsaturated Fatty Acids: 45:28 Have at least one double bond.
○​ Cholesterol: 47:40 (Sterol) Embedded in cell membranes to regulate fluidity.
●​ Proteins: 48:10
○​ Polymers made of amino acids.
○​ Amino Acid Structure: Central carbon, amine group, carboxyl group, hydrogen,
and R group (variable).
○​ Protein Structure:
■​ Primary: Sequence of amino acids.
■​ Secondary: Folding into alpha helices or beta-pleated sheets (hydrogen
bonds).
■​ Tertiary: Further folding into a 3D shape (hydrophobic/hydrophilic
interactions, hydrogen bonds, ionic bonds, disulfide bonds).
■​ Quaternary: More than one polypeptide chain.
○​ Fibrous Proteins: 51:24 Long, twisted strands (collagen, keratin, elastin).
○​ Globular Proteins: 51:53 Spherical shape (enzymes, antibodies, some hormones,
hemoglobin, pepsin, insulin).

4. Biochemical Tests 54:47

●​ Starch: Add iodine solution (orange-brown to blue-black).


●​ Reducing Sugars: Add Benedict's solution and heat (blue to green/yellow/orange/brick
red).
●​ Non-Reducing Sugars: 55:35 Boil with hydrochloric acid, neutralize with alkali, then add
Benedict's solution and heat (blue to green/yellow/orange/brick red).
●​ Proteins: Add biuret solution (blue to purple).
●​ Lipids: Emulsion test (dissolve in ethanol, add water, white emulsion forms).
●​ Colorimetry: 57:21 Use a colorimeter to measure the absorbance or transmission of light
through a sample.
●​ Biosensors: 58:06 Use immobilized DNA or protein to detect specific molecules.
●​ Chromatography: 58:30 Separates molecules based on their solubility in a solvent.
○​ Retention Factor (Rf): Distance moved by solute / Distance moved by solvent.

5. Nucleotides and Nucleic Acids 60:21

●​ Nucleotides: Monomers of nucleic acids (DNA and RNA).


○​ Nitrogenous Bases:
■​ Purines: (two rings) Adenine (A) and Guanine (G).
■​ Pyrimidines: (one ring) Cytosine (C), Thymine (T) (DNA), and Uracil (U)
(RNA).
○​ Pentose Sugar: Ribose (RNA) or deoxyribose (DNA).
○​ Phosphate Group.
●​ Base Pairing: A with T (or U in RNA), G with C.
●​ Phosphodiester Bond: 61:42 Bond between adjacent nucleotides in a nucleic acid chain.
●​ ATP (Adenosine Triphosphate): 62:17 Energy currency of the cell.
●​ DNA (Deoxyribonucleic Acid): 64:08
○​ Double helix structure.
○​ Stores genetic information.
○​ DNA Precipitation: 65:45 Homogenize cells, filter, add salt, add protease, add
ice-cold ethanol.
●​ RNA (Ribonucleic Acid): 66:34
○​ mRNA (messenger RNA): Carries genetic code from DNA to ribosomes.
○​ rRNA (ribosomal RNA): Component of ribosomes.
○​ tRNA (transfer RNA): Transports amino acids to ribosomes during protein
synthesis.
●​ DNA Replication: 69:10
○​ Semi-conservative: Each new DNA molecule contains one original strand and
one new strand.
○​ DNA Helicase: Unwinds the DNA double helix.
○​ DNA Polymerase: Adds nucleotides to the new DNA strand.
●​ Genetic Code Properties: 72:14
○​ Degenerate: Amino acids are coded for by more than one triplet of bases.
○​ Universal: The same triplet of bases codes for the same amino acid in all
organisms.
○​ Non-overlapping: Each base is part of only one codon.
●​ Protein Synthesis: 74:04
○​ Transcription: 75:50 mRNA is created from a DNA template in the nucleus.
○​ Translation: 77:05 mRNA is used to create a polypeptide chain on a ribosome in
the cytoplasm.
○​ Introns: Non-coding sequences in a gene that are removed from mRNA.
○​ Exons: Coding sequences in a gene.
○​ Start and Stop Codons: Initiate and terminate translation.

6. Enzymes 78:20

●​ Biological catalysts made of globular proteins.


●​ Active Site: 78:25 Specific shape that binds to the substrate.
●​ Lower activation energy of reactions.
●​ Lock and Key Hypothesis: 79:51 (Older model) Enzyme and substrate are perfectly
complementary.
●​ Induced Fit Hypothesis: 80:43 (Current model) Enzyme active site changes shape to fit
the substrate.
●​ Factors Affecting Enzyme Activity:
○​ Temperature: 82:35 Increases rate up to an optimum, then denatures the
enzyme.
○​ pH: 83:50 Enzymes have optimal pH ranges.
○​ Enzyme Concentration: 84:45 Increases rate up to a point of saturation.
○​ Substrate Concentration: 84:50 Increases rate up to a point of saturation.
●​ Enzyme Inhibitors: 86:27
○​ Competitive Inhibitors: 86:32 Similar in shape to the substrate and bind to the
active site.
○​ Non-Competitive Inhibitors: 88:24 Bind to the enzyme at a site other than the
active site (allosteric site), changing its shape.
○​ End-Product Inhibition: 89:27 The product of a reaction inhibits the enzyme.
●​ Coenzymes, Cofactors, and Prosthetic Groups: 90:13 Non-protein molecules required for
enzyme activity.
●​ Precursor Activation: 91:12 Enzymes are activated by a cofactor.
7. Biological Membranes 91:54

●​ Composed of a phospholipid bilayer.


●​ Fluid Mosaic Model: 92:10 Describes the structure and movement of components in the
membrane.
●​ Membrane Proteins:
○​ Extrinsic (Peripheral): On the surface.
○​ Intrinsic (Integral): Span the membrane (channel and carrier proteins).
●​ Cholesterol: 93:41 Regulates membrane fluidity.
●​ Factors Affecting Membrane Permeability:
○​ Temperature: 94:07 High temperatures increase fluidity and can denature
proteins.
○​ Solvents: 95:00 Organic solvents dissolve lipids, increasing permeability.
●​ Membrane Transport:
○​ Simple Diffusion: 95:33 Movement down a concentration gradient (no ATP
required).
○​ Facilitated Diffusion: 96:08 Movement down a concentration gradient with the
help of channel or carrier proteins (no ATP required).
○​ Osmosis: 96:45 Movement of water down a water potential gradient across a
partially permeable membrane.
○​ Active Transport: 98:33 Movement against a concentration gradient (ATP
required).
○​ Endocytosis: 99:39 Bulk transport of molecules into the cell (phagocytosis and
pinocytosis).
○​ Exocytosis: {timestamp:100:33} Bulk transport of molecules out of the cell.

8. Cell Division, Diversity, and Organization {timestamp:100:58}

●​ Cell Cycle: Interphase (G1, S, G2), nuclear division (mitosis or meiosis), cytokinesis.
●​ Mitosis: {timestamp:102:43} Creates two genetically identical diploid cells (growth, tissue
repair, asexual reproduction).
○​ Stages: Prophase, Metaphase, Anaphase, Telophase (PMAT).
○​ Cytokinesis: {timestamp:105:04} Division of the cytoplasm.
○​ Mitotic Index: {timestamp:107:06} Number of cells in mitosis / Total number of
cells.
●​ Meiosis: {timestamp:107:56} Creates four genetically different haploid daughter cells
(sexual reproduction).
○​ Two rounds of division (Meiosis I and Meiosis II).
○​ Crossing Over: {timestamp:108:55} Exchange of genetic material between
homologous chromosomes.
○​ Independent Assortment: {timestamp:110:02} Random alignment of homologous
chromosomes during metaphase I.
●​ Cellular Organization: {timestamp:111:30}
○​ Cells -> Tissues -> Organs -> Organ Systems -> Organism
●​ Specialized Cells: {timestamp:111:49} (e.g., epithelial cells, red blood cells, sperm cells,
xylem vessels, phloem sieve tubes, root hair cells).
●​ Tissues: {timestamp:112:34} (e.g., squamous epithelium, ciliated epithelium, muscle
tissue, cartilage,

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