What is a light microscope used for? | Observing living and dead specimins |
What are the pros and cons of a light microscope? | Pros: Cheap, portable, easy to use, can study living specimens. Cons: Limited magnification, poor resolution. |
What is a laser scanning confocal microscope used for? | Creating a high resolution, high contrast image, at different depths of the specimen. |
What is a transmission electron microscope be used for? | Observing the internal ultrastructure of cells under high magnification and resolution |
What is a scanning electron microscope used for? | Viewing the surface of objets under high magnification and resolution |
What are the pros and cons of an electron microscope? | Pros: Very high magnification and excellent resolution. Cons: specimen has to be dead, very expensive, very large, needs great skill and training to use. |
What is the difference between a transmission and an scanning electron microscope? | TEM sends a beam of electrons through the specimen, the SEM bounces electrons off the surface. |
What is the difference between light and electron microscopes? | Light uses lenses to focus a beam of light. Electron uses a beam of electrons, focused by magnets. |
What is an eye piece graticule? | A small ruler fitted to a light microscope's eyepiece. It must be calibrated using a stage micrometer before being used to measure specimens. |
What is a stage micrometer? | A millimeter long ruler etched onto a slide. it has 100 divisions, each of 0.01mm or 10 micrometers. It is used to calibrate the eyepiece graticule |
Why do we stain specimens? | To provide more contrast, and make it easier to distinguish certain parts. |
What is differential staining? | Using a stain to distinguish between either 2 different orgaisms, or between organelles of a specimin due to preferential absorbtion of stain. |
What is the formula to calculate magnification? | Magnification = Image size / Actual size |
What is the formula to calculate actual object size? | Actual size = Image size / Magnification |
How do we work out image size? | Use a ruler and measure the image. |
What is magnification? | A measure of how much larger the image of a specimen looks under the microscope |
What is resolution? | The ability to distinguish between to adjacent individual points as separate. |
What are the maximum resolutions of the different microscopes? | Light: 200nm; SEM: 10nm; TEM: 0.2nm. |
What is the maximum magnification of the different microscopes? | Light: 1,500X; SEM: 100,000X; TEM: 500,000X. |
What are the main structures of all eukaryotic cells? | Nucleus; nucleolus; cytoplasm; cytoskeleton; plasma membrane;mitochondria; Golgi apparatus; smooth endoplasmic reticulum; rough endoplasmic reticulum; ribosomes. |
What is the structure and function of the nucleus? | Surrounded by a double membrane (the nuclear envelope). Contains chromatin (DNA wound around histones). Stores the human genome, controls the cell by providing instructions for protein synthesis. |
What is the structure and function of the nucleolus? | Made of RNA, produces ribosomes. |
What is the structure and function of the nuclear envelope? | A double membrane embeded with channel proteins forming pores. Separates the nucleus from the rest of the cell. Pores allow ribosomes and mRNA to leave the nucleus. |
What is the structure and function of the rough endoplasmic reticulum (RER)? | A system of fluid filled membranes studded with ribosomes. Continuous with the nuclear membrane. Large surface area formed by folding, enables lots of protein synthesis. Proteins pinched off in vesicles transported to the Golgi apparatus. |
What is the structure and function of the smooth endoplasmic reticulum (SER)? | A system of fluid filled membranes. No ribosomes. Contain enzymes for cholesterol, lipid and phospholipid synthesis. |
What is the structure and function of the Golgi apparatus? | A stack of flattened membrane bound sacs. Vesicles from the RER join at the cis face. Here they are modified, by adding sugar to make glycoproteins, adding lipids to form glycolipids. Folding proteins into their 3D shape. Modified proteins are pinched off from the trans face into transport vesicles. |
What is the structure and function of the ribosomes? | 2 subunits, large and small. Made of rRNA . Proteins synthesised here. |
What is the structure and function of the mitochondria? | Double membrane bound. Inner membrane folded into cristae within a fluid filled matrix. Contain own DNA and 70s ribosomes. Site of aerobic respiration. |
What is the structure and function of the lysosomes? | Membrane bound sacs containing hydrolytic (digestive) enzymes. break down old organelles and foreign matter for reuse. |
What is the structure and function of the chloroplasts? | Double membrane bound. Inner membrane forms flat discs filled with chlorophyll called thylakoids, in stacks called granum. These are surrounded by a fluid matrix called the stroma. Contain own DNA and 70s ribosomes. Site of photosynthesis. |
What is the structure and function of the plasma membrane? | Phospholipid bilayer, cholesterol, proteins, glycoproteins, glycolipids. Separates cell contents from external environment. Controls what enters and leaves the cell. Identifies cell as self. Acts as a receptor for various chemicals. site of chemical reactions. |
What is the structure and function of the centrioles? | Present in animals only. Two bundles of microtubules at right angles. Used as an anchor point to separate chromosomes during cell division. Form the basis of cilia. |
What is the structure and function of the cell wall? | Present in plants and fungi only. Bundles of cellulose fibres in plants. Chitin in fungi. Provides support and strength, maintaining the cell's shape. prevents the cell from bursting when turgid. Permeable to allow solutions through. |
What is the structure and function of the flagella? | 9 pairs of microtubules surround 2 lone microtubules. A membrane covers the whole thing. Used for moving unicellular organisms around. |
What is the structure and function of the cillia? | 9 pairs of microtubules surround 2 lone microtubules. A membrane covers the whole thing. Present in great numbers. Move together in a wafting pattern to move single celled organisms. When present on tissues waft to move fluids such as mucus. |
Which structures are involved in the production of proteins? | Nucleus; RER; transport vesicle; Golgi apparatus |
What is the structure and function of the cytoskeleton? | Microfilaments made of actin - allow cell movement and cytokinesis. Microtubules made of tubulinsscaffold like structures to give cell shape. Intermediate fibres give mechanical strength, maintaining integrity. |
What do prokaryotic and eukaryotic cells have in common? | Plasma membrane; cytoplasm; ribosomes; DNa and RNA |
What is different between prokaryotic and eukaryotic cells? | Prokaryotes have no: Nucleus; centrioles; membrane bound organelles (mitochondria, chloroplast, RER, SER, Golgi apparatus). Prokaryotes also have: peptidoglycan cell wall; smaller ribosomes; naked loop of DNA; plasmids. |
How do prokaryotes divide? | Binary fission |
List out the elements that make up proteins. | C, H, O, N, S |
Explain the polar nature of water. | - O is more electronegative than H / unequal share of e- / e- spend more time orbiting around O than H |
What allows water molecules to have cohesive and adhesive properties? | Hydrogen bond |
Describe the structure of amylose, including the bonds involved and the shape. | All 1,4-glycosidic bonds, straight helix |
Describe the structure of amylopectin, including the bonds involved and the shape. | 1,4 and 1,6 glycosidic bonds, branched |
State the two structures that make up starch. | Amylose + Amylopectin |
State the reaction that breaks down maltose. | Hydrolysis |
What is the reaction to join monosaccharides together? | Condensation |
What are the 3 types of polysaccharides that α-glucose can form? | - Amylose |
What are the two monosaccharides that join up to make sucrose? | Glucose |
1,6 glycosidic bonds are found on ........ | Amylopectin |
β-glucose can only be found in ........ | Cellulose |
How are the monosaccharides in cellulose arranged? | Alternative β-glucose molecules are turned upside down |
Based on the arrangement of cellulose molecules, explain why cell walls provide strength and support to plant cells. | - cellulose molecules form hydrogen bonds with each other to make microfibrils |
What does the Benedict's test test for? | Reducing sugar |
Explain how a positive result is formed in Benedict's test. | Reducing sugar reacts with blue Cu2+ |
How can we test for starch? | Iodine solution |
How can we use a colorimeter to do a quantitative Benedict's test? | - Colorimeter measure the absorbance or transmission of light by a coloured solution |
What are the two parts that make up a carboxylic acid? | Carboxyl group + Hydrocarbon chain |
How many water molecule(s) is/are needed when breaking down a triglyceride? | 3 |
What is another term for the condensation reaction that makes lipids? | Esterification |
What is the difference in structure between saturated and unsaturated lipids? | - Saturated: all single C-C bonds in fatty acid chain |
Why do oils contain unsaturated triglycerides rather than saturated? | - Unsaturated fatty acids cause the molecule to kink/bend |
What is the difference in structure between triglyceride and phospholipid? | - phospholipid: 2 fatty acid chains + 1 phosphate group |
Describe the phospholipid bilayer arrangement. | - Hydrophilic heads point outwards |
Describe 2 similarities and 1 difference between phospholipids and sterols. | - Similarities: both have dual hydrophilic/hydrophobic characteristics / both make up the plasma membrane |
Describe the steps in identifying lipids and state the positive result. | - mix sample with ethanol |
State the monomer of a protein. | amino acids |
What are the components that make up an amino acid? | Central carbon + H atom + Amine group + Carboxyl group |
Name the bond formed between two amino acids. | Peptide bond |
What is the primary structure of a protein? | Amino acid sequence |
What is the secondary structure of a protein? | alpha-helix + beta-pleated sheets |
What is the tertiary structure of a protein? | Folding into a 3D shape |
What is the quaternary structure of a protein? | Binding with other subunits |
State the bond involved in the primary structure of a protein. | peptide bond |
Stat the bond involved in the secondary structure of a protein | hydrogen bond |
State the bond involved in the tertiary structure of a protein. | ionic, covalent, hydrogen, hydrophobic interactions, disulphide bridges |
State the bond involved in the quaternary structure of a protein. | ionic, covalent, hydrogen, hydrophobic interactions, disulphide bridges |
Name the reaction that breaks down proteins. | hydrolysis |
What is the solution used to test for the presence of proteins? | Biuret solution |
Describe a positive result for proteins. | Using Biuret solution: Blue to purple |
What is thin layer chromatography? | a technique to separate individual components of a mixture (eg. Amino acids) |
Based on what principles are the amino acids separated in TLC? | - depends on interactions (H bonds) aa form with silica in the stationary phase |
Why should the chromatography plate be only handled by the edges? | prevent contamination with proteins on hands |
What are the three types of proteins? | Globular, conjugated, fibrous |
Explain why insulin is soluble in blood. | Hydrophilic amino acids are folded on the protein surface |
What are prosthetic groups? | non-protein component in a conjugated protein |
Give an example of a conjugated protein. | Haemoglobin/Catalase |
Compare the haem groups in haemoglobin and catalase. | - Hb: Fe2+ bond reversibly with O2 in blood |
How many haem groups do a haemoglobin contain? | 4 |
Explain why keratin is relatively strong, inflexible and insoluble. | Many strong disulfide bridges |
Briefly describe the structure of collagen. | 3 polypeptides wound together in a long, strong rope-like structure |
What bonds do DNA/RNA polymerase catalyse? | Phosphodiester bonds |
Name the monomer of a nucleic acid. | Nucleotide |
State the five possible bases of a nucleotide. | Adenine, guanine, thymine, cytosine, uracil |
State the three components to a DNA nucleotide. | Deoxyribose + Nitrogenous base + Phosphate group |
The two strands of the double helix are ............. to each other. | antiparallel |
Thymine, cytosine and uracil belong to a group of bases. Name the group. | Pyrimidines |
Adenine and guanine belong to a group of bases. Name the group. | Purines |
State the complementary base pairings. | A-T/U, C-G |
State the number of hydrogen bonds formed between adenine and thymine/uracil. | 2 |
State the number of hydrogen bonds formed between cytosine and guanine. | 3 |
Why is DNA replication described as semi-conservative? | Each new DNA molecule is made up of one new and one old/template strand |
State the enzymes involved in DNA replication. | DNA helicase + DNA polymerase |
State the function of DNA polymerase. | Catalyses formation of phosphodiester bonds between DNA nucleotides |
State the function of DNA helicase. | Unzips DNA double helix, breaking hydrogen bonds |
The free nucleotides pair up with the exposed bases on the DNA strands based on ...... (which principle?) | Complementary base pairing |
DNA polymerase can only build phosphodiester bonds on the daughter strand in a particular direction. What is this direction? | 5' to 3' |
In which direction of the template strand does the DNA polymerase move in? | 3' to 5' |
Define 'genetic code'. | The sequence of bases in DNA that codes for the sequence of amino acids in protein production |
The genetic code is described as 'degenerate'. What does that mean? | Many different triplet codes/codons can code for the same amino acid |
Define 'gene'. | A section of DNA containing the base sequence that codes for a protein |
What is a codon? | Triplet bases on RNA |
What are the two differences between DNA and RNA? | - DNA has deoxyribose; RNA has ribose |
Name the enzymes involved in transcription. | DNA helicase + RNA polymerase |
Why is the antisense strand needed even though it does not code for proteins? | - it acts as the template strand |
What type of bond does mRNA have? | phosphodiester bonds |
Even though DNA codes for proteins directly, why is mRNA needed to be made for making proteins? | DNA is too large to leave the nucleus through the nuclear pores |
How is rRNA involved in catalysing translation? | - peptidyl transferase is an rRNA component |
Which part of tRNA binds to the mRNA? | anticodon loop |
Name the amino acid that is always at the start of a protein. | Methionine |
Describe what happens to the amino acid chain to make it a fully functional protein. | - The amino acid chain folds into secondary and tertiary structures |
State the two stages of protein synthesis. | Transcription + Translation |
Name the product of transcription. | mRNA |
Name the product of translation. | Polypeptide (then becomes functional protein after modification in Golgi) |
State the location where translation occurs. | Ribosomes |
What are the three main types of activities in cells that require energy? | Synthesis, transport, movement |
What does 'ATP' stand for and what is it? | Adenosine triphosphate, energy currency |
Draw the structure of ATP. | Ribose sugar (pentose with O on top) + adenine on C1 + 3 phosphate groups on C5 (must show C5 as an angle off the pentose sugar) |
How does ATP release energy? | ATP is hydrolysed into ADP + Pi, releasing energy |
State 3 properties of ATP. | Small - easy to move into and out of cells; Water-soluble; Releases energy in small quantities - so no heat loss; Easily regenerated by phosphorylation of ADP |
What are metabolic reactions? | the sum of all reactions in the organism |
What are anabolic reactions? | Building up larger molecules |
What are catabolic reactions? | Breaking down molecules |
What are enzymes? | Biological catalysts that speed up chemical reactions |
Name the energy that is required to start a reaction. | Activation energy |
What are enzymes' effect on the activation energy of a reaction? | Enzymes lower Ea |
Name the area on the enzyme that binds to and reacts with the substrate. | Active site |
The active site has a _____ shape to the substrate. | Complementary/Specific |
Name the two models used to illustrate enzyme actions. | Lock-and-key + Induced fit |
Name the structure where the enzyme and substrate are bound together. | Enzyme-substrate complex |
What is the difference between the lock-and-key model and the induced fit model? | Lock-and-key: rigid, no movement; Induced fit: slight movement of active site to allow better binding to substrate |
Name an intracellular enzyme. | Catalase |
Name an extracellular enzyme. | Amylase/trypsin |
Define the term ‘denaturation’. | Loss of active site shape |
Explain how an increase of temperature increases enzyme activity. | - Increasing temperature increases particles’ kinetic energy |
Explain how high temperatures can denature enzymes. | - High temperature leads to more vibrations |
What is the temperature coefficient (Q10)? | A measure of how much the reaction rate increases with a 10oC increase |
How are the enzymes in organisms that live in cold environments adapted? | - enzymes are more flexible, hence less stable |
How are the enzymes in organisms that live in hot environments adapted? | - enzymes are more stable (have more bonds in tertiary structure) |
How does a change in pH affect enzyme structure? | - A change in pH refers to a change in H+ concentration |
Explain why an increase in substrate concentration increases rate of reaction. | - Higher successful collision rate |
What does it mean by a ‘reversible’ inhibitor? | The inhibitor can be released from the enzyme to resume the enzymes’ function |
Most competitive inhibitors are reversible or irreversible? | Reversible |
Explain how Vmax of the enzyme can be unchanged in competitive inhibition. | - By adding more substrates to outcompete inhibitors |
What types of inhibitor does aspirin belong to? | Irreversible, competitive |
Explain the difference between competitive and non-competitive inhibition mechanisms. | - Competitive: inhibitor binds to active site à substrate can no longer bind to AS |
Explain how an increase in substrate concentration affects the rate of reaction in non-competitive inhibition. | No change |
State two examples of irreversible, non-competitive inhibitors for human use. | - Organophosphates à insecticides and herbicides (inhibits AChE) |
What is end-product inhibition? | The product of an enzyme-catalysed reaction acts as the inhibitor |
How does ATP regulate its own production by end-product inhibition? | - ATP binds to the allosteric site of PFK |
State the difference between cofactors and coenzymes. | - Cofactors = a non-protein component to help enzymes carry out their functions |
From which chemical are cofactors derived from? | Minerals |
From which chemical are coenzymes derived from? | Vitamins |
Name the cofactor found in amylase. | Chloride ion |
Name the cofactor invovled in photosynthesis. | NADP |
Name the cofactor invovled in respiration. | NAD + FAD |
State the difference between cofactors and prosthetic groups. | - Cofactors are temporarily bound to the enzyme |
Name the prosthetic group in haemoglobin. | Iron ion in haem group |
Name the prosthetic group in carbonic anhydrase. | Zn2+ |
What are the three ways that an enzyme can be activated by changing the tertiary structure? | - Adding a cofactor |
Why is it important that some enzymes are produced in its inactive form? | Otherwise it may damage the cell it was produced in |
What is an apoenzyme? | Inactive form of enzyme |
What is a holoenzyme? | Active form of enzyme |
What is the fluid mosaic model? | The theory of the cell membrane formed from a sea of phospholipids emmeded with proteins. |
What is a glycolipid? | A lipid with a carbohydrate molecule attached. |
What is a glycoprotein? | A protein with a carbohydrate molecule attached. |
State four functions of membranes at the surface of cells | Compartmentalisation (separates cell's components from its external surroundings ensuring conditions inside cell remain unaffected); regulates transport of material into and out of cells (endocytosis and exocytosis); has surface antigens so the body's immune system recognises the cell as 'self'; contains receptors for chemical signals (hormones, drugs etc); may be the site of chemical reactions |
State 3 functions of membranes within cells | Compartmentalisation (maintains specific conditions for metabolic reactions to take place, e.g. photosynthesis in chloroplasts, aerobic respiration in mitochondria); inner mitochondrial membrane is highly folded providing a larger surface area for electron carrier proteins; thylakoid membranes within chloroplasts house chlorophyll, the primary pigment required for light absorption in photosynthesis; vesicle production. |
The principal design of the plasma membrane consists of two layers; what name is given to these two layers? | Phospholipid bilayer |
Explain the orientation of phospholipids within the bilayer | Hydrophilic phosphate heads are orientated outwards (towards water); hydrophobic fatty acid tails are orientated inwards (away from water) |
Describe the function of glycoproteins and glycolipids in the phospholipid bilayer | As markers or antigens; cell signalling; cell communication; call adhesion |
Give 3 examples of intrinsic proteins | Channel proteins, carrier proteins, glycoproteins |
Channel proteins and carrier proteins have what main role within the membrane? | Transport |
Describe the position and role of cholesterol in the membrane | Interspersed between phospholipid molecules; regulates fluidity of membrane by coming between phospholipids preventing crystallisation. Also bonds to phospholipids, preventing it becoming too fluid. |
Describe the structure of a phospholipid | Glycerol backbone; one hydrophilic phosphate head; two hydrophobic fatty acid tails |
Describe the effects of temperature on membrane structure | As temperature increases, phospholipids will have more KE, so move faster and more, making the bilayer more fluid and it begins to lose its structure. This loss of structure allows molecules to cross it more easily. Carrier and channel proteins may become denatured, affecting membrane transport. |
Describe the effects of ethanol on membrane structure | Non-polar ethanol molecules can insert themselves into the bilayer (hydrophobic tails) disrupting the structure, meaning the bilayer becomes more fluid and permeable |
Explain why alcohol is used in antiseptic wipes. | Alcohol can disrupt and dissolve bacteria's membrane due to their non-polar nature, killing them |
Define the term diffusion. | The net movement of a substance from an area of high concentration to an area of low concentration. It is passive, does NOT require ATP. |
Define the term facilitated diffusion | Movement of molecules from a high concentration to a low concentration, across a partially permeable membrane, via specific channel or carrier proteins. It is passive, does NOT require ATP |
What is a channel protein? | A protein which creates a fluid filled pore in the cell membrane through which ions and small polar molecules can pass. |
What is a carrier protein? | A protein which changes shape to allow larger molecules to pass through the membrane. In facilitated diffusion this requires no energy, in active transport it requires ATP. |
What types of molecules can diffuse directly across the phospholipid bilayer? | Small molecules such as oxygen and carbon dioxide; lipid-soluble molecules such as steroid hormones and alcohol |
Describe the movement of water across the phospholipid bilayer | Water is polar and insoluble in lipid, BUT because it is present in such high quantities, significant direct, simple diffusion does occur. In membranes (e.g. collecting duct) where a very high rate of water movement is required, special channel proteins known as aquaporins are inserted into the membrane. |
State 5 factors that affect the rate of simple diffusion | Temperature, surface area, diffusion distance, size of molecule, concentration gradient |
Define the term active transport | Movement of molecules, against their concentration gradient (using energy liberated from ATP hydrolysis) using specific protein channels or carriers |
Describe how carrier proteins are used in active transport | Molecule binds to specific site in carrier protein; ATP binds to separate binding site; carrier protein changes shape (conformational change) and transports molecule across membrane |
Define bulk transport and give two examples | The movement of large molecules that are too big to pass across the plasma membrane. Endocytosis (phagocytosis or pinocytosis) brings large molecules INTO the cell, enclosed in a vesicle. Exocytosis transports large molecules OUT of cells. |
Define and describe phagocytosis | The intake of solid particles into the cell by engulfing. Pseudopodia surround the particles, the membrane fuses together, to form a vesicle. |
Define and describe pinocytosis | The intake of liquids into the cell by engulfing. The plasma membrane invaginates, and the membrane fuses around the substance, forming a vesicle. |
Define and describe exocytosis | The bulk transport of particles too large to pass through the membrane, out of the cell. It works like a reversal of pinocytosis. A vesicle containing the substance fuses with the plasma membrane. The fused site opens, releasing the contents of the secretory vesicle. |
Describe the role of ATP in bulk transport | ATP is required to provide energy for the movement of vesicles along microtubules of cytoskeleton (via motor proteins); ATP is needed to fuse vesicle membrane and plasma membrane together (PM is changing shape) |
What is the main difference between active transport and facilitated diffusion? | Active transport requires ATP; facillitated diffusion is passive |
Define the term osmosis | The movement of water molecules from a region of higher water potential to a region of lower water potential, across a partially permeable membrane |
What is water potential? | The tendancy of water molecules to move from one region to another. |
What substance has the highest possible water potential of 0 kPa? | Pure water |
State the equation that links water potential, solute potential and pressure potential | WP = SP + PP |
As more solute is added to a solution, what happens to the solute potential and hence the water potential? | Solute potential decreases, hence water potential decreases |
Describe what would happen to a red blood cell placed in a solution with a more negative water potential than that of its cytoplasm | Water would move OUT, down a WP gradient, shrinking to crenation |
Describe what would happen to a liver cell placed in a solution with a more positive WP than its own cytoplasm | Water would move IN, down a WP gradient, swelling the cell and causing it to burst (CYTOLYSIS) due to the presence of no cell wall |
Describe what would happen to a root hair cell placed in a solution with lower WP than its own cytoplasm/vacuole | Water would move OUT, down a WP gradient, causing the cell to become flaccid and then plasmolysed |
Describe what would happen to a guard cell placed in a solution of less negative WP than its own cytoplasm | Water would move IN, down a WP gradient, causing the cell to swell and become TURGID |
State three events that occur in G1 phase of the cell cycle | Cells grow and increase in size; proteins from which organelles are made are synthesised (transcribed and translated); organelles replicate |
What happens during the S phase of the cell cycle? | This is the synthesis phase, DNA is replicated. |
What happens during the G2 phase? | Second growth phase, proteins which involved in making the chromosomes condense are synthesised (transcribed and translated). |
Describe what may happen in G0 phase of the cell cycle | Cells may undergo apoptosis, differentiation or senescence |
State three cell cycle checkpoints and briefly describe what is being checked for at each | G1/S - checks for size, growth factors, nutrients, DNA damage; G2/M - checks DNA has been properly replicated; spindle assembly - checks chromosomes have correctly attached to spindle fibres |
State three purpose of mitosis in life cycles | Asexual reproduction; growth; tissue repair; replacement of cells |
Describe the main events of phophase | Nuclear envelope breaks down; chromatin condenses (DNA supercoils); nucleolus disappears; spindle fibres start to form from centrioles |
Describe the main events of metaphase | Chromosomes line up along equator (metaphase plate); spindle fibres attach through centromeres |
Describe the main events of anaphase | Sister chromatids pulled to opposite poles of the cell by shortening tubulin spindle fibres |
Describe the main events of telophase | Nuclear envelope reforms around each set of chromosomes; chromatin relaxes; nucleolus reappears |
Describe how cytokinesis differs between dividing animal cells and plant cells | Animal cells - cleavage furrow forms and plasma membrane is pulled inwards, splitting the cytoplasm; plant cells - vesicles assemble around metaphase plate and fuse; new plasma membrane and cellulose cell wall are laid down |
Why would we use the root tip for investigating mitosis? | It is the location of meristematic tissue (source of stem cells) in a plant, i.e. cells are actively dividing |
Explain why we warm the root tips in hydrochloric acid when preparing a root tip squash | To break the links between cellulose cell walls in plant cells; this ensures the stain penetrates the cells and binds to the chromosomes |
Which stain would we use to stain chromosomes in a root tip squash? | Acetic orcein |
What is meiosis? | The formation of gametes. Genetically unique with half the genetic information of a somatic cell. |
Describe how meiosis produces genetic variation in the gametes produced | Crossing over in prophase I; independent assortment in metaphase I; independent assortment in metaphase II |
Describe the difference between anaphase I and anaphase II | In anaphase I, a homologous pair of chromosomes is separated so the chromosome number halves (2 haploid cells made); in anaphase II, sister chromatids of each chromosome are separated so chromosome number stays the same (haploid number maintained) |
In which stage of meiosis is the chromosome number halved | Anaphase/telophase I |
Explain why genetic variation is important for a population of organisms | More likely that some individuals are adapted to a change in the environment, so the population can survive |
What is differentiation? | The process by which a cell develops to become more distinct in form and function |
Describe and explain how erythrocytes are adapted for their function | Very small so have a large SA:vol (biconcave shape also ensures this) meaning oxygen can reach all regions inside the cell; well-developed cytoskeleton allows the erythrocytes to change shape and move through very narrow capillaries; no nucleus or organelles so more space for Hb molecules |
Explain why a neutrophil contains many lysosomes | These contain hydrolytic enzymes which digest pathogens |
Describe and explain how sperm cells are adapted for their function | Acrosome in head contains enzymes to penetrate the egg follicle during fertilisation; many mitochondria to generate ATP for flagellar movement; large haploid nucleus in head to fertilise haploid ovum |
Describe how guard cells open in sunny conditions | Light energy --> ATP; ATP used to actively transport potassium ions from epidermal cells into guard cells; water potential of guard cells lowered; water moves in by osmosis and guard cells become turgid |
Describe the purpose of cytoskeleton threads and motor proteins in palisade cells | Moves the chloroplasts to areas of appropriate light intensity |
Describe how a root hair cell plasma membrane is adapted for transport of mineral ions | Contains specialised carrier proteins to transport specific mineral ions in by active transport |
Describe how cartilage is adapted for its function | Connective tissue that contains elastin and collagen fibres; prevents ends of bones from rubbing together |
Define the term tissue | A group of cells working together to perform a particular function |
State three types of muscle tissue, giving an example of where each is found | Skeletal - bicep/tricep etc.; smooth - digestive tract, blood vessels; cardiac muscle - heart walls |
Give four features of meristematic cells that means they can differentiate easily | Thin walls with very little cellulose; no chloroplasts; no large vacuole; divide by mitosis and have the ability to differentiate into many cell types |
Describe the differences between multipotent, pluripotent and totipotent stem cells | Multipotent - found in bone marrow and can form a range of different cells including blood cells; pluripotent - found in early embryos (embryonic stem cells) and can form all tissue types except extra-embryonic cells; totipotent - found in first 16 cells post-zygote and can form all tissue types including extra-embryonic tissue (e.g. placenta, umbilical cord) |
State three characteristics of stem cells | Undifferentiated; all genes able to be expressed; self-renewing; able to differentiate into any cell type |