IBDP Biology

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163 Terms

1
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Discuss possible exceptions to cell theory (4)

- skeletal muscle fibres have many nuclei

---cells always function as autonomous units

- aseptate fungal hyphae have a continuous cytoplasm

---living structures are composed of discrete cells

- giant algae (unicellular) grow to very large sizes

---larger organisms are always made up of many microscopic cells

2
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State the functions of one named extracellular component (4)

plant cell wall:

- strengthens/supports cell

- maintains shape of cells

- prevents pathogen entry

3
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Explain the importance of surface area:volume ratio (6)

- large surface area:vol needed

- as cells increase in size ratio is reduced (volume increases faster than surface area)

- surface area needs to be large enough to absorb nutrients/oxygen/substances needed

- needs to be large enough to excrete/pass out waste products

- optimum diffusion is large surface area and small volume

- cells divide when they reach a certain size

4
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Outline differentiation of cells in a multicellular organism (6)

- differentiation is development in different/specific ways

- cells carry out specialised functions/become specialised

- some genes are expressed/switched on but not others

- regulated mainly during transcription

- chemicals determine how a cell develops

- becomes more efficient

- group of differentiated cells = tissue

5
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Describe the importance of stem cells in differentiation (4)

- stem cells are undifferentiated cells

- stem cells retain capacity to divide and differentiate along different pathways into specialised cells

- differentiation involves expressing some genes but not others

- stem cells can be used to repair/replace tissue/heal wounds

6
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Describe stem cells and how they are used in medicine (stargardt's) (5)

- stem cells are undifferentiated and retain capacity to divide

Stargardt's:

- genetic degeneration of photoreceptor cells in retina

- human embryonic stem cells treated to differentiate into retinal cells

- retinal cells injected into area

- they attach and become functional - improves vision

7
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Describe stem cells and how they are used in medicine (leukemia) (6)

- stem cells are undifferentiated and retain capacity to divide

Leukemia:

- cancer of blood/bone marrow

- hematopoeic stem cells harvested from the bone marrow

- chemotherapy/radiotherapy used to destroy diseased WBCs

- HSCs transplanted back into bone marrow

- differentiate to become WBCS and replace diseased ones

8
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Draw a labelled diagram to show the ultrastructure of E.coli (6)

- cell wall

- plasma membrane

- cytoplasm

- flagellum (embedded in cell wall)

- 70S ribosomes

- nucleoid/naked DNA

9
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Compare adult and embryonic stem cells (5)

embryonic:

/ almost unlimited in growth potential

/ less chance of genetic damage

X more risk of becoming tumor

X chance of rejection (diff from recipient)

X ethics - extraction kills embryo

adult:

/ less chance of developing tumors

/ extraction does not kill adult

/ no rejection issues

X difficult to obtain (few + deep)

X less growth potential

X limited capacity to differentiate

10
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Function of cell wall

Protect against mechanical and hypertonic stress

11
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Function of plasma membrane

phospholipid layer controls movement of materials in/out

12
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Function of nucleoid region

storage of genetic info (genetic info) and DNA replication

13
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Function of ribosomes

site of protein synthesis

14
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Function of flagella

movement and sexual conjugation

15
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Function of cytoplasm

where metabolic reactions occur

16
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How do prokaryotic cells divide (4)

Binary Fission:

- single circular chromosome replicated

- 2 copies move to opposite ends

- division of cytoplasm = genetically identical daughter cells

- CYTOKINESIS

17
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Draw a labelled diagram of a eukaryotic cell (6)

- golgi apparatus

- free 80S ribosomes

- mitochondrion

- lysosomes

- centrioles

- rough ER

- vesicles

- nucleus

- vacuole

- plasma membrane

18
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Function of golgi apparatus

sorting and transporting proteins

19
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Describe the process of tRNA activation (4)

- specific tRNA activating enzyme recognises specific amino acid

- enzyme binds ATP to amino acid

- specific tRNA molecule recruited

- tRNA binds to amino acid (AMP released)

- ATP phosphorylation creates high energy bond - transferred to RNA

- provides energy for peptide bond to form during translation

20
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Function of lysosomes

digestion/metabolism of materials ingested by endocytosis using digestive enzymes

21
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Function of centrioles

move chromosomes during cell division

22
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Function of rough ER

protein synthesis and transport

23
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Function of nucleus

controls cell activities/DNA replication/DNA transcription/mitosis

24
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Function of vacuole

Digestion, storage, waste disposal, water balance

25
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Function of vesicle

Small vacuoles used to transport materials inside cell

26
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Explain the advantages of compartmentalization (5)

= membrane bound organelles

1. Efficiency of metabolism (enzymes/substrates more concentrated)

2. localised conditions (e.g. pH maintained at ideal)

3. toxic substances isolated (e.g. digestive enzymes in lysosome)

4. numbers/locations of organelles can be changed

27
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Distinguish between the structure of plant and animal cells (6)

plant cells:

- have cells walls

- have chloroplasts

- large central vacuole

- store starch

animal cells:

- have centrioles

- have cholesterol in membrane

28
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Compare prokaryotic cells and eukaryotic cells (5)

Size: p = small, e = large

compartmentalized: p = no, e = yes

ribosomes: p = 70s, e = 80s

dna structures: p = naked, no histones e = bound to histones

site of dna: p = nucleoid, e = nucleus

mitochondria: p = no, e = yes

29
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Draw a labelled diagram to show the structure of the plasma membrane (5)

- phospholipid bilayer

- phospholipid (hydrophobic fatty acid tail, hydrophilic phosphate head)

- integral protein

- glycoprotein

- channel protein

- peripheral

- cholesterol

30
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Explain how the structure and properties of phospholipids help to maintain the structure of cell membranes (9)

- hydrophobic tail/hydrophilic head

- form bilayer (hydrophilic exterior hydrophobic interior)

- held together by hydrophobic interactions

- layers stabilised by interactions of hydrophilic heads and surrounding water

- phospholipids can move about to increase fluidity

- allow for membrane fluidity

- fluidity helps be functionally stable

- fluidity important in making/breaking membranes (endo/exocytosis)

- layers restrict entry/exit of substances

31
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Explain the role of cholesterol in the plasma membrane (4)

- component of plasma cell membranes

- positioned between phospholipids in the membrane

- reduces membrane fluidity and permeability to some solutes

- disrupts regular packing of hydrocarbon tails

- prevents crystallisation and solid behavior

- help membranes curve into concave shape (formation of vesicles)

32
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Explain the role of vesicles in the transportation of materials within cells (8)

- vesicles are membrane bound packages

- formed by pinching off a piece from membrane (endocytosis)

- can carry proteins

- RER synthesizes proteins - proteins accumulate in ER - vesicles bud off RER

- vesicles transport to Golgi apparatus

- fuse to GA, process protein into final form

- bud off GA move to plasma membrane

- protein secreted by exocytosis

33
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Describe the process of active transport (4)

- uses/requires ATP

- against concentration gradient

- uses protein

- protein goes through conformational change

- ATP is hydrolysed -> ADP

34
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Outline the ways in which a substance can move passively across a membrane (5)

- diffusion is a method of passive transport

- channel proteins in facilitated diffusion allow hydrophilic molecules to cross

- movement from high to low conc gradient

- e.g. oxygen

- osmosis is diffusion of water through a membrane

- region of higher water potential to lower

35
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Describe simple diffusion (2)

passive net movement of particles from area of high concentration to low concentration often through a partially permeable membrane

- non polar small particles (e.g. oxygen) diffuse easily

36
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Describe facilitated diffusion (2)

Movement of large and polar molecules that can't get across the membrane via simple diffusion through transmembrane proteins

37
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Describe osmosis (2)

Passive net movement of water molecules from low solute conc. to area of high solute conc. through partially permeable membrane

(sometimes through protein aquaporin)

38
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Distinguish between passive and active movements of materials across plasma membranes, using named examples (4)

passive: diffusion, osmosis, f diffusion

active: ion pumps, exocytosis, endocytosis, active transport

a = requires energy, p = does not

a = against conc g, p = down conc g

a = protein required, p = no protein required

a = e.g. root cell ion uptake, p = oxygen alveoli

39
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Outline, with example, the process of exocytosis (5)

- vesicles carry materials to the plasma membrane

- vesicle fuses with plasma membrane

- by joining of phospholipid bilayers

- aided by fluidity of the membrane

- material released/expelled from cell

- membrane flattens

e.g. hormone secretion

- hormones released have an effect on another cell

40
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Explain the reasons for cell division in living organisms (8)

- increase number of cells in an organism

- allow differentiation/cell specialization

- for greater efficiency

- and replace damaged/lost cells

e.g. binary fission

- asexual reproduction of unicellular organisms

- gamete/spore formation

- cells cannot grow beyond certain size

- sa:vol ratio becomes too small

- transport across membrane is too slow

41
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Outline the processes that occur in a cell during interphase, including those needed for mitosis (4)

Interphase: active period in cell cycle when many metabolic reactions occur in nucleus and cytoplasm

- dna replication

- organelle duplication

- cell growth

- transcription/translation

- obtain nutrients

- respiration

42
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Outline the 3 stages in interphase (3)

G1 - cell grows and preps for DNA replication

S - synthesis stage - DNA replicated

G2 - cell finishes growing and preps for cell division

43
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Describe the cell cycle (8)

1. Prophase

- DNA supercoils and chromatin condense

- centrosomes move to opposite cell poles and form microtubule spindle fibers

- nuclear membrane breaks down

2. Metaphase

- microtubule spindle fibers connect to centromeres of each chromosome

- spindle fibres contract and chromosomes align along center of cell

3. Anaphase

- contraction causes sister chromatids to separate

- move to opposite poles of cells

4. Telophase

- spindle fibers dissolve

- chromosomes uncoil, decondense

- nuclear membranes reform

44
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Describe process of cytokinesis (4)

process of cytoplasmic division

- mt filaments form ring around cell center

- constrict and form cleavage furrow

- furrow meets center and is pinched off

- 2 cells formed

45
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Explain the role of cyclins (5)

- regulatory proteins that control progression of cell cycle

- bind to enzymes called cyclin-dependent kinases

- activate them and CDK attaches phosphate groups to other proteins in the cell

- triggers other proteins to become active and carry out tasks in cell cycle

- 4 main cyclins -> have to reach certain concentration before progressing to next stage

46
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Outline the evidence for endosymbiotic theory (4)

- organelles originated as symbioses between separate single-celled organisms

- contain own circular DNA (like prokaryotes)

- 70S ribosomes

- only produced by division of pre-existing mitochondria/chloroplasts

- transcribe DNA and use mRNA to synthesize own proteins

47
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Outline the thermal, cohesive and solvent properties of water (5)

- high specific heat capacity

- large amount of heat causes small increase in temperature

- high latent heat of vaporization

- large amount of heat is required to vaporize

- cohesive (due to hydrogen bonds)

- good solvent (water molecules are polar)

48
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Describe the significance of water to living organisms (5)

adhesion - allows plants to transport water up during transpiration

cohesion - allows high surface tension - insects can move on surface

good solvent - can dissolve substances for transportation in organisms

high LOV - good coolant

high SHC - thermally stable aquatic habitats

49
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Describe the use of carbohydrates and lipids for energy storage in animals (5)

carbohydrate

- stored as glycogen in liver

- short-term energy storage

- more easily digested so energy released quickly

lipid

- stored as fat in animals

- long-term energy storage

- more energy per gram than carb

50
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List three functions of lipids (3)

- energy storage

- insulation

- internal organ protection

- buoyancy

- component of cell membranes

- electrical insulation - myelin sheath

- hormones (steroid)

51
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Describe the significance of polar and non-polar amino acids (5)

polar:

- hydrophilic

- can make hydrogen bonds

- found on surface of water-soluble protein

non-polar

- hydrophobic

- found in interior of water soluble proteins

- found in protein in interior of membrane

52
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Draw and describe the structure of a glucose molecule (3)

C6H12O6

- 6-membered ring

- side chain

- hydroxyl group points _ _ ^ _

<p>C6H12O6</p><p>- 6-membered ring</p><p>- side chain</p><p>- hydroxyl group points _ _ ^ _</p>
53
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Draw and describe the structure of a ribose molecule (3)

C5H10O5

- 5 membered ring

- side chain

- ^ _ _ hydroxyl group

<p>C5H10O5</p><p>- 5 membered ring</p><p>- side chain</p><p>- ^ _ _ hydroxyl group</p>
54
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Draw and describe the structure of a saturated fatty acid (3)

- unbranched chain

- single bonds (saturated)

- no. carbon atoms = 14-20

- one end = carboxyl group

<p>- unbranched chain</p><p>- single bonds (saturated)</p><p>- no. carbon atoms = 14-20</p><p>- one end = carboxyl group</p>
55
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Draw and describe the structure of a generalised amino acid (3)

carbon bonded to:

- amine group

- carboxyl group

- hydrogen atom

- R group

<p>carbon bonded to:</p><p>- amine group</p><p>- carboxyl group</p><p>- hydrogen atom</p><p>- R group</p>
56
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Draw and describe the formation of disaccharide (3)

glucose + glucose -> maltose + H2O

- via condensation reaction

<p>glucose + glucose -> maltose + H2O</p><p>- via condensation reaction</p>
57
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Draw and describe the formation of a triglyceride (6)

1 fatty acid + 3 glycerol = triglyceride (via condensation)

- held by ester bond

- composed of C, H, O

- non-polar hydrophobic molecule

- saturated if all are C-C

<p>1 fatty acid + 3 glycerol = triglyceride (via condensation)</p><p>- held by ester bond</p><p>- composed of C, H, O</p><p>- non-polar hydrophobic molecule</p><p>- saturated if all are C-C</p>
58
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Outline the types of carbohydrates and their functions with examples (5)

Monosaccharides

- Energy source

e.g. glucose, galactose, fructose

Disaccharides

- transport form

e.g. lactose, sucrose, maltose

Polysaccharides

- storage form

e.g. cellulose, glycogen, starch

59
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Outline the features of cellulose (5)

- beta-glucose subunit

- 1-4 glycosidic bond

- unbranched

- straight shape

- function = cell walls

60
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Outline the features of amylose (5)

- alpha glucose subunit

- 1-4 glycosidic bond

- unbranched

- helix shape

function = energy storage

61
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Outline the features of amylopectin (5)

- alpha glucose subunit

- 1-4 & 1-6 bond

- branched

- globular shape

function = energy storage

62
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Outline features of glycogen (5)

- alpha glucose subunit

- 1-4 & 1-6 bond

- branched

- more compact shape than starch

- energy storage (humans)

63
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Outline the difference between saturated and unsaturated fatty acids (3)

- fatty acids are long hydrocarbon chains

saturated = single bonds and linear, solid @ room temp

unsaturated = double bonds, bent, liquid @room temp

64
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Outline the role of hydrolysis and condensation in the relationship between amino acids and dipeptides (4)

- condensation: water produced when 2 amino acids joined

- hydrolysis - water needed to break bond

<p>- condensation: water produced when 2 amino acids joined</p><p>- hydrolysis - water needed to break bond</p>
65
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Describe the structure of proteins (9)

- primary = chain of amino acids

- each position occupied by one of 20 diff amino acids

- linked by peptide bonds

- secondary = interaction between amino and carboxyl (N-H and C=O)

- weak hydrogen bond formed

- alpha helix/beta pleated sheet forms

- tertiary = folding of polypeptide

- stabilised by disulfide bridges/hydrogen/ionic bond

- quarternary = several polypeptide subunits join

- some combine with non-protein molecules

66
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List 6 functions of proteins, giving examples of each (4)

STRUCTURE

- connective tissue of animals

e.g. collagen

HORMONES

- e.g. insulin

- hormone that triggers reduction in blood glucose levels

IMMUNITY

e.g. immunoglobin

- antibody that targets specific antigens

TRANSPORT

- nutrients and gases, e.g. hemoglobin

SENSATION

- receptors e.g. rhodopsin in eyes

- pigment that detects light

MOVEMENT

- muscle contraction (actin and myosin)

ENZYMES

- e.g. Rubisco

- enzyme catalysing CO2 fixation

67
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Distinguish between cis and trans isomers (3)

cis: hydrogen atoms attached to C=C on same side

trans: hydrogen atoms attached to C=C on different side

- produced by hydrogenation (bad!)

68
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Distinguish between fibrous and globular proteins with reference to one example of each (6)

- f = strand/sheets, g = ronuded

- f = usually insoluble, g = usually soluble

- g = more sensitive to change in pH

- f = have structural roles

- g = function roles (e.g. transport)

- f = e.g. collagen

= g = e.g. hemoglobin

69
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Explain 3 reasons for converting lactose to glucose and galactose during food processing (3)

- allows people who are lactose intolerant to consume milk products

- galactose/glucose taste sweeter than lactose - reduce need for extra sweetener

- more soluble (smoother texture, reduce crystallization in ice cream)

- bacteria ferments them quicker - faster yogurt production time

70
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Outline how enzymes catalyse reactions (7)

- increase rate of chemical reaction

- without being changed itself

- lowers activation energy

- due to kinetic energy and random collisons

- substrate joins with enzyme at active site

- substrate is complementary shape to active site

- forms enzyme substrate complex

- active site/enzyme is specific for particular substrate

-

71
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Explain the effect of pH on enzyme activity (3)

- enzymes have optimal pH

- lower activity below and above optimum (graph)

- too high/low can denature enzyme

- change shape of active site/alter tertiary structure

- substrate cannot bind to active site - ESC cannot form

72
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Compare the induced fit model of enzyme activity with the lock and key model (4)

- both models substrate binds to active site

- both - ESC forms

- L = substrate fits exactly, I = fit is not exact

- L = active site does not change shape, I = changes shape

- L = binding reduces EA, I = substrate reduces EA

- I explains competitive inhibition (L does not)

73
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Outline the advantages of using immobilized enzymes (4)

an enzyme fixed to a static surface to improve efficiency of a catalysed reaction

- easily separated from products of reaction

- enzymes can be recycled

- increases enzymes stability (less prone to pH/temp change)

- substrates can be exposed to higher enzyme conc = faster reaction rate

74
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Explain, using one example, the effect of a competitive inhibitor on enzyme activity (6)

- has similar shape/structure to substrate

- fits to active site

- substrate cannot bind as long as inhibitor is bound

- only 1 active site per enzyme molecule

- inhibitor and substrate compete for active site

- high substrate concentrations can overcome inhibitor

e.g. ethanol and alcohol dehydrogenase

75
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Explain, using one example, the effect of a non-competitive inhibitor on enzyme activity (6)

- inhibitor has different shape to substrate

- binds to allosteric site

- causes conformational change on active site

- substrate cannot bind with enzyme

- substrate cannot prevent binding even at high conc

e.g. cyanide + cytochrome oxidase

76
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Discuss the solubility of proteins in water (4)

- depends on what amino acids/R groups are present

- smaller proteins are more soluble than big ones

- proteins with many polar R groups are more soluble

- globular proteins are more soluble than fibrous

- affected by ph/temp

- denaturation make proteins insoluble

77
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Outline enzyme-substrate specificity (5)

- active site of enzyme binds to specific substrate

- shape of substrate and active site complement

- lock and key

- chemical properties of substrate and enzyme attract

- induced fit

- active site is not rigid - substrate can induce slight changes in shape

- causes weakening of bonds in substrate to lower EA

78
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Explain how proteins act as enzymes, including control by feedback inhibition in allosteric enzymes (9)

- enzymes are globular proteins

- there is active site

- substrate binds to active site

- shape of substrate and active site is changed

- bonds in substrate weakened

- activation energy reduced

- in feedback inhibition end product binds to enzyme

- end product is substance produced in last/later stage of a pathway

- inhibitor product binds to allosteric site

- causes active site to change shape

- substrate no longer fits active site

- higher conc of end product lowers enzyme activity

- whole pathway is inhibited

- prevents build up of intermediates

79
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Define trophic level

- feeding level for an organism in a food chain

80
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Compare the ways in which autotrophic, hetertrophic and saprotrophic organisms obtain energy (6)

- autotrophs use external energy source e.g. light

- heterotrophs obtain energy from other organisms

- usually ingest/consume food

- saprotrophs obtain energy from non-living matter/dead organisms

- saprotrophs digest organic matter extracellularly

81
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Describe the relationship between the rise in concentration of atmospheric CO2 and the enhanced greenhouse effect (5)

- CO2 is a greenhouse gas

- increase in CO2 enhances greenhouse effect

- earth receives short wave radiation from sun

- reradiated from Earth as longer wave radiation

- CO2 absorbs longer wave radiation

- global warming happened same time as CO2 increase

- CO2 conc correlated positively with global temperature

82
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Distinguish between unique and highly repetitive sequences in nuclear DNA (5)

U: occur once in genome, H: occur many times

U: long base sequences, H: short base sequences

U: may be genes, H: not genes

U: translated/coding sequences, H: never translated

U: small differences between individuals, H: can vary greatly

U: exons, H: introns

U: smaller genome prop., H: larger genome prop

- repetitive sequences used for profiling

83
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Draw a labelled diagram of the structure of DNA (5)

- 4 nucleotides (one labelled)

- base, phosphate and deoxyribose labelled

- correct carbons labelled

- backbone labelled (covalent bond, 3-5 end)

- 2 base pairs linked by hydrogen bonds drawn as dotted lines

- 2 H bonds between A and T

- 3 H bonds between G and C

- antiparallel orientation shown

<p>- 4 nucleotides (one labelled)</p><p>- base, phosphate and deoxyribose labelled</p><p>- correct carbons labelled</p><p>- backbone labelled (covalent bond, 3-5 end)</p><p>- 2 base pairs linked by hydrogen bonds drawn as dotted lines</p><p>- 2 H bonds between A and T</p><p>- 3 H bonds between G and C</p><p>- antiparallel orientation shown</p>
84
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Explain the structure of the DNA double helix, including its subunits and the way in which they are bonded together (8)

- subunits are nucleotides

- one base, one deoxyribose and one phosphate in each nucleotide

- deoxyribose linked to C1, phosphate to C5

- 4 different bases (adenine, thymine, cytosine, guanine)

- covalent phosphodiester bonds

- 2 strands of nucleotides linked together

- base to base

- A-T, C-G

- hydrogen bonds between bases

- antiparallel strands

- double helix

85
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Outline the structure of the nucleosome in eukaryotic chromosomes (4)

- contain histones

- 8 histone molecules form a cluster

- DNA strand wound around histones

- wound twice around each nucleosome

- histone molecule holds nucleosome in place

86
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State a role for each of the 4 different named enzymes in DNA replication (6)

HELICASE

- unwinds DNA

DNA polymerase III

- adds nucleotides in 5' to 3' direction extending existing strand

RNA PRIMASE

- synthesizes short RNA primer on DNA (initiation point for DNA pol III)

DNA polymerase I

- replaces RNA primer with DNA nucleotides

DNA ligase

- joins Okazaki fragments on lagging strand (joins sugar-phosphate backbones with phosphodiester bond)

87
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Explain the process of DNA replication (8)

- occurs during S phase of interphase in prep for mitosis

- semi-conservative

- unwinding of double helix by helicase at replication origin

- hydrogen bonds between 2 strands are broken

- each strand of parent DNA used as template of synthesis

- continuous on leading strand but not on lagging strand

- leads to formation of Okazaki fragments on lagging strand

- synthesis from 5-3' direction

- RNA primase synthesizes RNA primer on parent DNA

- DNA pol III adds nucleotides to 3' end

- added according to complementary base pairing

- adenine-thymine, cytosine - guanine

- DNA pol I removes RNA primers and replaces with DNA nucleotides

- DNA ligase joins Okazaki fragments

88
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Describe how the process of DNA replication depends on the structure of DNA (9)

- dna molecule is double stranded

- hydrogen bonds linking two strands can be broken

- DNA can be split into two strands by helicase

- backbones are linked by covalent bonds - so strands do not break and base sequence is conserved

- base pairing is complementary

- A=T and C=G

- 2 original strands carry same info

- 2 new strands have same base sequence as 2 original

- base nucleotides added in 5-3' diretion

- strands have opposite polarity (antiparallel)

89
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Outline what is meant by semi-conservative replication (3)

DNA replication is semi-conservative and depends on complementary base pairing

- 2 DNA molecules, 1 original and 1 newly synthesized

- ensures strands are identical in base sequence to replicated parent molecule

90
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Describe the genetic code (6)

- composed of mRNA base triplets called codons

- 64 codons

- each codes for the addition of an amino acid to a polypeptide chain

- genetic code is degenerate

- i.e. more than one codon can code for a particular amino acid

- genetic code is universal

- i.e. same in all organisms

- AUG is the start codon

- some codons code for the end of translation

91
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Discuss the relationship between genes and polypeptides (5)

- originally assumed that one gene = one polypeptide = one mRNA

- many more proteins made than genes available

- some genes do not code for polypeptide

- some code for tRNA/rRNA

- some regulate gene expression

- polypeptides may be altered before becoming functional proteins

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Explain briefly the advantages and disadvantages of the universality of the genetic code to humans (4)

- genetic material can be transferred between species/humans

- one species can use useful gene from another

- transgenic crop plants/livestock can be produced

- bacteria/yeast can be genetically engineered (useful)

X viruses can invade cells and take over genetic apparatus

X viruses cause disease

93
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Compare the processes of DNA replication and transcription (9)

SIMILARITIES

- unwinding of helix

- separating 2 strands

- breaking hydrogen bonds between bases

- complementary base pairing involved

- C-G pairing

- 5'-3' direction

- linking of nucleotides

- start signal required

DIFF:

- R = DNA nucleotides, T = RNA molecules

- R = deoxyribose nucleotide, T = ribose nucleotide

- R = A-T, T = A-U

- R = both copied, T = 1 copied

- diff start signal

- R = 2 DNA molecules, T = mRNA

94
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Distinguish between RNA and DNA (3)

- DNA is double stranded while RNA is single stranded

- DNA contains deoxyribose, RNA contains ribose

- Thymine in DNA, Uracil in RNA

- one form of DNA (double helix) but several forms of RNA (mRNA, tRNA, rRNA)

95
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Describe the roles of mRNA, tRNA and ribosomes in translation (6)

- mRNA contains genetic code

- ribosomes have large subunit and small subunit

- tRNA with amino acid attached

- tRNA with anticodon

- mRNA held by ribosome

- 2 tRNA molecules attached to mRNA on ribosome

- peptide bond forms between amino acids on tRNA

- polypeptide forms

- continues until stop codon is reached

- polypeptide is released

96
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Define transcription

The synthesis of mRNA copied from the DNA base sequence by RNA polymerase

97
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Outline the structure of tRNA (5)

- one chain of RNA nucleotides

- has site for attaching amino acid

- at 3' end

- has anticodon

- of 3 unpaired bases forming a loop

- double stranded sections formed by base pairing

- has cloverleaf shape

- 3 loops

98
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Outline the structure of ribosome (4)

- large subunit and small subunit

- mRNA binding site on small subunit

- 3 tRNA binding sites (E, P, A)

- made of protein and ribosomal RNA

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Outline the use of Taq DNA polymerase (5)

- used to produce multiple copies of DNA rapidly by polymerase chain reaction

1. Denaturation - heating to 95 C to separate 2 strands

2. Annealing - sample cooled to 54C, primers designate sequence to be copied

3. Elongation - heated to 75 C, Taq polymerase can function optimally (extends nucleotide chain from primers)

4. cycle repeated

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Outline the role of tandem repeats in DNA profiling (4)

variable number tandem repeat = short nucleotide sequence that shows variations between individuals in terms of no. of times sequence is repeated

- restriction enzymes used to cut DNA between tandem repeats

- electrophoresis to calculate length of tandem repeat

- profiling!