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GRADE 12 > BIOLOGY EXAM > Flashcards

BIOLOGY EXAM Flashcards

1
Q

What are functional groups?

A

A functional group is a group of atoms that affect the function of a molecule; usually ionic and strongly polar

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2
Q

What are the 7 functional groups?

A

Aldehyde, ketone, carboxyl, amino, phosphate, sulfhydryl, hydroxyl

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3
Q

What is a hydrogen bond?

A

The attractive force between a partial positively (δ+) charged hydrogen atom to a partial negatively (δ-) charged atom – only N, O, or F atoms

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4
Q

What is a glycosidic linkage?

A

a bond between 2 monosaccharides. These bonds are formed by dehydration synthesis reactions and most commonly bind from the hydroxyl group on carbon 1 on the first monosaccharide and hydroxyl group on carbon 4 on the second monosaccharide.

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5
Q

What is a phosphodiester linkage?

A

Link that is formed between nucleotides by a phosphate bridge; the phosphate group of one nucleotide is linked by a phosphodiester bond to the deoxyribose of the adjacent nucleotide.

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6
Q

What is a dehydration reaction?

A

Used to assemble small molecules together into larger ones. The removal of -OH from one reactant and -H from the other reactant form water; the rest of the other two reactants from a new compound.

Reactant (with -OH) + Reactant (with -H) -> Product + Water

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7
Q

What is a hydrolysis reaction?

A

used to break a large molecule into smaller molecules with the addition of water. Water is a reactant that splits the other reactant molecule into a product with -OH and a product with -H.

Reactant + Water -> Product (with -OH) + Product (with -H)

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8
Q

What is an enzyme?

A

a protein that changes the rate of a chemical reaction without being changed themselves

Ex. amylase speeds up the hydrolysis of amylose (starch) into maltose.

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9
Q

What is a substrate?

A

A substance that is recognized by and binds to an enzyme. They tend to be much smaller than the enzyme and interact with the specific groove on the enzyme called an active site.

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10
Q

What is the induced-fit hypothesis?

A

Enzymes will change shape so that the active site is more percise to bind to the specified substrate. The reaction proceeds, and the enzyme will release the products from the enzyme-substrate complex, leaving the enzyme unchanged and ready to bind again.

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11
Q

What is the purpose of carbohydrates?

A

sources of short term energy, building materials and cell communication

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12
Q

What are the 3 types of carbohydrates?

A

monosaccharides, disaccharides, and polysaccharides

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13
Q

What is a monosaccharide?

A

Single sugar and simplest carbohydrate. It is distinguished by a carbonyl group (an aldehyde, called an aldose, or a ketone, called a ketose) and length of carbon chain (3 carbons-triose,
5 carbons-pentose, and 6 carbons-hexose)

Ex. glucose, fructose

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14
Q

When shape is a monosaccharide if it is in a dry state?

A

Linear

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15
Q

What shape is a monosaccharide if it is dissolved in water

A

Ring

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16
Q

What are the 2 configurations of the carbohydrate ring?

A

alpha 𝛂 configuration and beta 𝜷 configuration

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17
Q

What is alpha configuration?

A

The OH group on #1 carbon is below the plane

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18
Q

What is beta configuration?

A

The OH group on #1 carbon is above the plane

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19
Q

What is a dissacharide?

A

2 monosaccharides joined together by a dehydration reaction via 1-4 glycosidic linkage.

Ex. maltose, lactose, sucrose

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20
Q

What is a polysaccharide? What shape can they take? What are their properties?

A

formed by linking monosaccharides by glycosidic linkages. They can be straight chained or branched. Polysaccharides are very polar and hydrophilic, however their size makes them insoluble in water.

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21
Q

Which specific carbohydrates (polysaccharides) are important for energy storage?

A

Starch and glycogen

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22
Q

What is the purpose of starch?

A

main energy storage for glucose in plants.

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23
Q

What is the purpose of glycogen?

A

main energy storage for glucose in animals.

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24
Q

Which carbohydrates (polysaccharides) are important for structural support?

A

Cellulose and chitin

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25
Q

What is the purpose of cellulose?

A

major component of cell walls and provides rich supply of energy to organisms. Humans cannot digest cellulose because they lack the enzyme.

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26
Q

What is the purpose of chitin?

A

forms exoskeleton of mushrooms, insects, and crustaceans; used for contact lenses and biodegradable stitches.

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27
Q

What is the purpose of lipids?

A

most common energy-storing molecules, provide twice as much energy as carbohydrates.
major component of cell membranes in living organisms.

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28
Q

What are the properties of lipids?

A

non-polar molecules and hydrophobic

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29
Q

What are the 5 types of lipids?

A

fatty acids, fats, phospholipids, steriods, waxes

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30
Q

What is the structure of a fatty acid?

A

consists of a carboxyl group and a hydrocarbon chain

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31
Q

What are the 2 types of fatty acids and fats?

A

saturated and unsaturated

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32
Q

What is a saturated fatty acid/fat?

A

Contain single bonds between carbons; easily stack

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33
Q

What is a unsaturated fatty acid/ fat?

A

Has one or more double bonds between carbons, which causes kinks

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34
Q

What is the structure of a fat?

A

consists of a glycerol molecule and fatty acids. Glycerol is a 3 carbon carbon alcohol with a hydroxyl group on each carbon. Glycerol forms the backbone of fats, to which 3 fatty acids are attached by a dehydration reaction via an ester linkage.

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35
Q

What is the purpose of phospholipids?

A

primary lipids of cell membranes in living organisms.

Ex. in the cell membrane

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36
Q

What is the structure of phospholipid?

A

It is made of a glycerol backbone, 2 fatty acids, and a charged phosphate group. The fatty acid tail is hydrophobic and the phosphate + polar unit head is hydrophilic.

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37
Q

What is the purpose of proteins?

A

extremely essential for structural support, movement, storage, immune system, transport materials, signalling, enzymes

Ex. immunoglobulins, hemoglobins, keratin, fibrin, collagen

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38
Q

What is denaturation?

A

This is a structural change in proteins due to an increase in temperature or changes in pH, that results in an altered function/dysfunction.

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39
Q

What is the structure of an amino acid?

A
  1. A central carbon
  2. An amino group
  3. A carboxyl group
  4. An H atom
  5. A side chain (R group)
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40
Q

How many amino acids are there?

A

There are a total of 20 amino acids; 12 can be synthesized by our cells, 8 are considered essential and must be obtained from our diet.

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41
Q

What is a polypeptide chain?

A

Amino acids connected by peptide bonds. Each polypeptide has a C-terminus (carboxyl end) and a N-terminus (amino end)

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42
Q

What are the 4 levels of structure in protein?

A

primary, secondary, tertiary, quartnernary

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43
Q

What is the primary structure of a protein?

A

specific linear sequence of amino acids; if one amino acid is changed in the sequence, it could render the protein dysfunctional.

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44
Q

What is the secondary structure of a protein?

A

folds and coils at various locations of the polypeptide due to hydrogen bonding between electronegative N and O atoms and partially positive H-atoms. There are 2 different orientations: alpha helix and beta pleated sheet.

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45
Q

What is the 𝛂 helix shape?

A

coiled shape, H bonds form between the carboxyl group and the amino groups of amino acids along the same chain (every 4 amino acids)

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46
Q

What is the 𝜷 pleated sheet shape?

A

2 separate polypeptide strands that run parallel to each other interact due to H bonds, an accordion shape appears.

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47
Q

What is the tertiary structure in proteins?

A

3D structure is determined by intermolecular reactions between R groups in the polypeptide chain. Intermolecular reactions include ionic bonds, hydrophobic interactions, hydrogen bonds, or disulfide bridges.

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48
Q

What is quarternary structure?

A

Some proteins consist of 2 or more polypeptide chains aggregated into one functional macromolecule. The final structure is critical as its orientation and shape is directly related to its function.

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49
Q

What is the purpose of nucliec acids?

A

Informational macromolecules that stores hereditary information

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50
Q

What is the structure of nucliec acids?

A

nucleic acids are polymers of monomers called nucleotides linked together by dehydration synthesis reactions via phosphodiester bonds.

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51
Q

What are the 3 components of nucleotides?

A
  1. nitrogenous bases
  2. pentose
  3. phosphate groups
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52
Q

What are the 2 types of nitrogenous bases? What is their shapes?

A
  1. Pyrimidine: 6 membered, single ring of C and N (cytosine, thymine, and uracil)
  2. Purine: 5 membered ring fused to a 6 membered ring (adenine and guanine)
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53
Q

What are the 2 types of pentose?

A
  1. Ribose: sugar in RNA with oxygen
  2. Deoxyribose: sugar in DNA without an onxygen
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54
Q

Where is the phosphate group attached to in the nucleotide?

A

5 carbon of the pentose

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55
Q

What is passive transport? What are the 3 types?

A

movement of molecules in biological systems that doesn’t require energy. Particles move from high to low concentration (with the concentration gradient). Passive transport includes simple diffusion, faciltated diffusion, and osmosis.

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56
Q

What is simple diffusion?

A
  • movement of molecules from an area of high to low concentration unassisted
  • can occur across cellular membranes if the solutes are small enough
  • influenced by temperature and pressure
  • rate of diffusion steadily increases
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57
Q

What is facilitated diffusion?

A
  • occurs if the rate of diffusion is too slow or if the cell needs ions and large polar molecules
  • diffusion of these molecules across a membrane occurs with the help of transmembrane proteins called transport proteins
  • the rate of diffusion is influenced by the concentration gradient, the efficiency of transport molecules, or the number of transport proteins
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58
Q

What is osmosis? What are the 3 types of solutions?

A

movement of water across semi permeable membrane; occurs when the membrane is impermeable to the solute in question. The 3 types of solutions include hypotonic, hypertonic, and isotonic.

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59
Q

What is a hypotonic solution?

A

if the extracellular solution is lower in solute concentration than the inside of the cell, water will move INTO the cell, causing it to expand; bursting is possible as well.

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60
Q

What is a hypertonic solution?

A

if the extracellular solution is higher in concentration than the inside of the cell, water will move OUT of the cell, causing it to shrivel.

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61
Q

What is an isotonic solution?

A

solute concentration both inside and outside the cell is equal so water moves in and out of the cell at an equal rate.

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62
Q

What is active transport? What are the 4 types of active transport?

A

This process requires cell energy to move materials in and out of the cell; particles move from high concentration to low concentration (against the concentration gradient) There are 4 types of active transport that inlcude, primary active transport, secondary active transport, endocytosis, and exocytosis.

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63
Q

What is primary active transport?

A

identical to facilitated diffusion except for the fact that the molecules move against the concentration gradient, which requires ATP

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64
Q

What is seconary active transport? What mechanism is it facilitated by?

A

uses the concentration gradient of an ion, created by an electrochemical gradient. It is facilitated by symport and antiport.

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65
Q

What is symport?

A

a solute moves through the membrane channel in the same direction as the driving ion.

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66
Q

What is antiport?

A

driving ions move through membranes in one direction, providing energy for active transport of another solute in the opposite direction.

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67
Q

What is endocytosis?

A

the process of importing large molecules or even whole cells from the exterior of the cell into the cytosol. There are 3 types of endocytic pathways: pinocytosis, receptor-mediated, and phagocytosis.

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68
Q

What is pinocytosis?

A

cells engluf extracellular water and any other molecules in the solution.
(cell drinking)

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69
Q

What is receptor-mediated endocytosis?

A

outer cell contains surface receptor proteins that recognize and bind to specific molecules, bringing them into the cell.

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70
Q

What is phagocytosis?

A

cells engulf solid particles
(cell eating)

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71
Q

What is exocytosis?

A

large molecules held within the cell are transpotyed to the external environment

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72
Q

What is oxidation?

A

an atom LOSES an electron. The reducing agent is the molecule being oxidized and losing electrons.

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73
Q

What is reduction?

A

an atom GAINS an electron. The oxidizing agent is the molecule being reduced and gaining electrons.

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74
Q

What is endergonic reactions?

A

a chemical reaction in which energy is ABSORBED, giving the products MORE potential energy than the reactants.

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75
Q

What is exergonic reactions?

A

chemical reaction in which energy is RELEASED; the product has LESS potential energy than the reactants.

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76
Q

What is the overall goal of glycolysis?

A

6C glucose is split into 3C

glucose + 2 ADP + 2 Pi +2 NAD+ -> 2 pyruvate + 2 ATP +2 NADH

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77
Q

Where does glycolysis occur?

A

cytoplasm

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78
Q

What is the net ATP prodcued in glycolysis? How many NAD+ are reduced to NADH? What are other products of glycolysis?

A

2 ATP net
2 NADH
2 pyruvate

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79
Q

What is the first step of pyruvate oxidation?

A

The carboxyl group from pyruvate is removed to form CO₂.

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80
Q

What is the overall goal of pyruvate oxidation?

A

2 pyruvates (from glycolysis) become 2 molecules of Acetyl-CoA.

2 pyruvate + 2 NAD+ + 2 CoA -> 2 Acetyl-CoA + 2 NADH + 2 H+ + 2 CO₂

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81
Q

What is the second step of pyruvate oxidation?

A

2e- and 2H+ are transferred to NAD+, reducing it to 2 NADH + H+

82
Q

What is the third step of pyruvate oxidation?

A

A sulfur-containing compound called coenzyme A (CoA) bonds to the acetyl group, producing Acetyl-CoA which will then enter the Krebs cycle.

83
Q

Where does pyruvate oxidation occurs?

A

mitochondrial matrix

84
Q

What is the overall goal of krebs cycle?

A

all of the C atoms in glucose have been completely consumed.

oxaloacetate + Acetyl-CoA + ADP + Pi + 3 NAD+ +FAD -> CoA + ATP + 3 NADH

85
Q

What is the total yield for 2 cycles of the krebs cycle?

A

4 CO₂
2 ATP
6 NADH
2 FADH

86
Q

What is the overall goal of ETC and Chemiosmosis?

A

to build a proton gradient (high concentration of H+) and a proton-motive force (called an electrochemical gradient) in the intermembrane space of the mitochondria for ATP synthesis.

87
Q

Where does the ETC occur?

A

inner mitochondrial membrane

88
Q

What begins the CR ETC?

A

Oxygen begins the movement of electrons by interacting with the last protein complex; 2 electrons are removed. Together the 2 electrons, oxygen, and 2H+ from the matrix forms water.

89
Q

What supplies electrons for the first and second protein complex in the CR ETC?

A

The oxidation of NADH, reduces the first protein complex. The oxidation of FADH2, reduces the second protein complex.

90
Q

What happens to the electrons after the protein complexes are reduced? How is an electrochemical gradient established? (In CR ETC)

A

As the electrons are shuttled down from one protein complex to the next, protons (H+ ions) are pumped out into intermembrane space and create an electrochemical gradient. Electrons shuttle through the ETC until they reach the final electron acceptor, oxygen.

91
Q

What is chemiosmosis?

A

process where ATP is created using an electrochemical gradient

92
Q

How is ATP produced through chemiosmosis (CR ETC)

A

The electrochemical gradient causes H+ ions to flow back into the matrix (with concentration gradient) through the ATP Synthase Complex
As H+ pass through it powers enzyme which allows ATP to form from ADP and Pi (reserve in the matrix)

93
Q

What is the purpose of the light reations and what is the location?

A

The purpose is to capture light energy to produce ATP and NADPH (energy carriers). Occurs in thylakoid membranes of chloroplasts.

94
Q

What are the 3 parts of the light reactions

A

photoexcitation, noncyclic elctron transport, and chemiosmosis

95
Q

What is photoexcitation?

A

an electron in chlorophyll absorbs a photon (light energy) that excites the electron which allows them to move between the different photosystems.

96
Q

What is Photosystem I?

A

absorbs wavelengths that are 700 nm. This is the second photosystem in the ETC, but it was the first photosystem discovered. Electrons reaching PSI are re-excited by light energy, which passes to an electron acceptor and then to the transport system, where NADP+ is reduced to NADPH.

97
Q

What is photosystem II?

A

absorbs wavelengths that are 680 nm. This is the first photosystem in the ETC. Chlorophyll P680 in PS II absorbs energy. The boosted electron moves through a transport system that releases energy (H+) for the production of ATP. Electrons fill the “hole” left by electron boost of PS I. Electrons from splitting of water fills the “hole” left in PSII and produces oxygen as a by-product. P680+ (PSII) is very electronegative – it can pull electrons from H 2 O molecules and split them! These electrons, along with an enzyme subunit called the water-splitting complex, reduce P680+ to P680 returning it to its neutral state and able to be oxidized again.

98
Q

Describe the process of non-cyclic electron transport (PSSN)

A
  • Chlorophyll P680 in PSII absorbs light energy
  • Boosted electron moves through a transport system that releases energy for the production of ATP
  • Electron fills the “hole” left by electron boost of PS I
  • Electron from splitting of water fills the “hole” left in PSII and produces oxygen as a by- product
  • P680 + (PS II) is very electronegative – it can pull electrons from H2O molecules and split them. These electrons in the water-splitting complex reduce P680 + to P680 returning it to its neutral state and able to be oxidized again.
  • Chlorophyll P700 in PS I absorbs light energy
  • Energy “hole” is filled by the electron from PS II
  • Boosted electrons from PS I pass to an acceptor, then to the transport system.
  • Finally, the electron, and an H+ ion from the stroma joins with NADP+ to form NADPH.
  • NADPH is the final electron acceptor and is used in the Calvin Cycle.
  • A proton gradient is formed as the H + ions accumulate in the thylakoid lumen from:
    1) splitting of water
    2) the pumping of H + into the thylakoid lumen from the stroma.
  • This gradient produces electrochemical energy that will be used to make ATP.
  • Protons move through the ATP synthase complex, forming ATP since light is required for ATP formation, the process is called photophosphorylation. ATP will be used in the Calvin Cycle.
  • Considered to be non-cyclic because once an electron is lost by a reaction centre it does not return to that system, as it ends up in NADPH
99
Q

Describe the process of chemiosmosis in photosynthesis

A

A proton gradient is formed as the H + ions accumulate in the thylakoid lumen from 1) splitting of water and 2) the pumping of H + into the thylakoid lumen from the stroma. This gradient produces electrochemical energy that will be used to make ATP. Protons move through the ATP synthase complex, forming ATP (from ADP + Pi).

100
Q

What are the key players in the light reactions?

A
  • Photosystem II (PSII): Captures light to excite electrons and split water.
  • Electron Transport Chain (ETC): Transfers electrons and pumps H+
  • Photosystem I (PSI): Re-excites electrons and reduces NADP+ to NADPH.
  • ATP Synthase: Produces ATP from ADP + Pi.
101
Q

What is the overall yield of the light reactions?

A
  • ATP and NADPH (used in dark reactions).
  • Oxygen (O2) as a by-product
102
Q

How many turns of the calcin cycle is require to make 1 G3P molecule for glucose? Where do the light-independent reactions occur? What are the 3 stages?

A

3 turns; occurs in the stroma of chloroplasts; the 3 stages include carbon fixation, reduction reactions, RuBP regeneration

103
Q

What is carbon fixation?

A
  • CO₂ is added to RuBP (ribulose 1, 5-bisphosphate) which is a 5 carbon molecule to form a 6 carbon intermediate.
  • This 6 carbon will then split into two 3 carbon molecules of PGA (3-phosphoglycerate). This first reaction occurs 3 times to produce 6 molecules of PGA.
  • All the reactions in this phase are catalyzed by the enzyme RuBisCO
104
Q

What are the reduction reactions?

A
  • Each PGA is phosphorylated from the hydrolysis of 6 ATP to create 6 molecules of 1,3-BPG (1,3-bisphosphoglycerate)
  • NADPH is oxidized to NADP+. The 2 e- from each of the 6 NADH reduce 1,3-BPG to G3P (3-phosphoglycerate)
  • 6 Pi molecules are released and can go back to the light reactions to make more ATP
  • Only 1 of the 6 G3P is used to make glucose and other organic molecules.
105
Q

What is the RuBP regeneration?

A
  • The remaining 5 G3P are combined and rearranged to form 3 molecules of RuBP
  • 5 molecules of G3P x 3 carbons per G3P = 15 carbons
  • 15 carbons / 5 carbons per RuBP = 3 RuBP molecules
  • The production of 1 glucose molecule requires 2 G3P, so it would take 6 turns of the calvin cycle to produce 1 glucose molecule.
106
Q

What is photorespiration?

A

an unfavorable process which decreases the production of sugars by photosynthesis. In hot, dry environments, guard cells decrease the size of stomata opening in order to conserve water. This decreases the CO₂ in the leaves, while increasing the O₂. O₂ now competes with CO₂ for rubisco’s active site, and since there is more oxygen, it binds to RuBisCO more often. This results in the oxidation of RuBP, instead of its carboxylation to PGA which decreases the production of carbohydrates. Photorespiration is not ideal because it requires more ATP and resources, slows the Calvin Cycle down due to the increase in substeps, and releases carbon (CO₂) back into the air.

107
Q

What makes up the back bone of DNA?

A

sugar and phosphate group

108
Q

What bonds are used in DNA? Where are they found?

A
  • ester bond: phosphate and sugar (phosphate group and #5 carbon)
  • glycosyl bond: sugar and nitrogenous base (base and #1 carbon)
  • hydrogen bond: nitrogenous bases on both strands
  • phosphodiester bond: between nucleotides (phosphate group and adjacent #3 carbon)
109
Q

What are the complimentary base pairs in DNA?

A

AT and CG

110
Q

What is a codon?

A

a triplet of bases that will code for a specific amino acid.

111
Q

What is the start codon?

A

AUG (methionine)

112
Q

Describe Step 1 of DNA replication

A
  • DNA replication begins at specific sites known as origins of replication. In order to efficiently replicate long strands of eukaryotic DNA, there are multiple replication origins.
  • A special enzyme called HELICASE recognizes the origins of replication and starts breaking the hydrogen bonds between nitrogenous bases.
  • The double stranded DNA begins to unwind into single strands. As they separate, they form a Y- shaped structure, called THE REPLICATION FORK
  • While the DNA is being unwound, tension is created. This is relieved by a class of enzymes called TOPOISOMERASES. These enzymes will relieve the tension by cutting and rejoining strands near the replication fork.
  • Once separated, the complementary bases have a tendency to rejoin. SINGLE-STRANDED BINDING PROTEINS(SSBs) will prevent this by attaching to the strands, and preventing H-bonds from reforming (annealing)
  • Separation can occur in both directions from a replication origin creating a replication bubble. This allows for more efficient replication.
113
Q

What are the 3 steps in DNA replication?

A
  1. seperating the DNA strands
  2. building the complementary strands
  3. proofreading and repairing errors
114
Q

Describe Step 2 of DNA replication

A
  • DNA polymerases add nucleotides to the 3’ end of a new developing complementary DNA strand. DNA POLYMERASE III reads the parent strand only in the 3’ to 5’ direction.
  • DNA polymerase builds the new strand using NUCLEOSIDE TRIPHOSPHATE, similar to the nucleotides in finished DNA. (Energy is needed for the new strand to be built, this energy is provided by removing 2 phosphates from the nucleoside triphosphate)
  • DNA polymerase III cannot begin adding nucleotides without an attachment point. RNA PRIMASE builds a small complementary RNA segment (RNA primer) on the parent template strand at the 3’ end.
  • The strands are built in the 5’ to 3’ direction in two different ways:
  • LEADING STRAND – the template parent strand that begins at the 3’ end. Therefore, the complementary strand is continuously made moving toward the replication fork.
  • LAGGING STRAND– the template parent strand that begins at the 5’ end. Therefore, the complementary strand is made discontinuously in short segments called OKAZAKI FRAGMENTS.
  • DNA replication is discontinuous on the lagging strand because the replication fork must open first before nucleotides can be added. Therefore, every time the fork is opened further, another RNA primer is required at the 3’ end before DNA polymerase III can add nucleotides.
  • RNA primers are replaced with DNA nucleotides by DNA POLYMERASE I.
  • Finally, DNA LIGASE catalyzes the reaction that connects the DNA segments together, including the Okazaki fragments, by a phosphodiester bond.
115
Q

What is the leading strand?

A

the template parent strand that begins at the 3’ end. Therefore, the complementary strand is continuously made moving toward the replication fork.

116
Q

What is the lagging strand?

A

the template parent strand that begins at the 5’ end. Therefore, the complementary strand is made discontinuously in short segments called OKAZAKI FRAGMENTS.

117
Q

Describe Step 3 of DNA replication

A
  • DNA polymerase III will proofread each nucleotide as it is being added. If there is a mistake, the enzyme functions as an exonuclease where it backtracks and replaces the wrong nucleotide before continuing on.
  • DNA polymerase II will work to repair any damage to DNA that occurs between replication events.
  • DNA polymerase I will fill the gaps with the correct nucleotide bases and DNA ligase connects
118
Q

What is the central dogma?

A

DNA is TRANSCRIBED into complementary messenger RNA, and ribosomes TRANSLATE messenger RNA into a specific sequence of amino acids, which are used to build proteins

119
Q

What is RNA and the 3 types of RNA?

A

RNA: A carrier of genetic information, similar to DNA. There are 3 major types of RNA:
- mRNA (messenger RNA)
varies in length, depending on the gene that has been copied
acts as the intermediary between DNA and the ribosomes
translated into proteins by ribosomes
RNA version of the gene encoded by DNA
- tRNA (transfer RNA)
functions as the delivery system of amino acids to ribosomes as they synthesize proteins
very short, only 70-90 base pairs long
- rRNA (ribosomal RNA)
binds with proteins to form the ribosomes
varies in lengths

120
Q

What are the 4 steps of transcription?

A
  1. initiaion
  2. elongation
  3. termination
  4. post-transcriptional modifications
121
Q

Describe transcription intiation

A

RNA polymerase binds to the DNA and unwinds starting at the promoter. More specifically, RNA polymerase binds to the TATA box because it has a high percentage of adenine and thymine, which only have 2 hydrogen bonds that are easy to break.

122
Q

Describe transcription elongation

A

RNA polymerase continues transcribing as it begins to build the single strand RNA molecule without a primer. RNA is made in the 5’ to 3’ direction using the 3’ to 5’ strand called the template strand. The opposite DNA strand is referred to as the coding strand, as it contains the exact same sequence as the RNA molecule. While RNA polymerase is transcribing, another RNA polymerase may start transcription again at the promoter.

123
Q

Describe transcription termination

A

Transcription of a gene is terminated when the RNA polymerase recognizes a termination sequence. RNA transcript is released and RNA polymerase is free to bind to another promoter region. The termination sequence is a string of adenines, which makes up the Poly-A tail

124
Q

Describe post-transcriptional modifications

A

The transcribed RNA is a precursor to mRNA and is vulnerable to conditions outside of the cell nucleus. It must be modified by a Poly-A tail, a 5’ Cap and splicing.
- Poly-A polymerase adds a chain of 50-250 adenines to the 3’ end of the pre-mRNA, producing the Poly-A tail, which allows for it to be translated efficiently and protects it from attacks of enzymes in the cytosol.
- The 5’ Cap, a sequence of 7 guanines, are added to the start of the pre-mRNA which functions as the initial attachment site that the ribosome recognizes and will use.
- An enzyme-protein complex called a spliceosome excises introns (a non-coding sequence of DNA/RNA) and splices the exons (sequence of DNA/RNA that codes for a gene) together.

125
Q

What are the 3 stages of translation?

A
  1. intiation
  2. elongation
  3. termination
126
Q

Describe translation initiation

A

Small and large ribosomal subunits associate with an mRNA molecule at the 5’ cap and an initiator tRNA. The first tRNA for initiation has the anticodon UAC that binds to the AUG (Methionine) start codon on mRNA
Step 1: Initiator Met-tRNA forms a complex with the small ribosomal subunit
Step 2: The complex binds to the mRNA 5’ cap. It will move along the mRNA until it reaches the AUG start codon
Step 3: The start codon is recognized by the anticodon of the Met-tRNA and the large ribosomal subunit binds to complete the ribosome at the P-site.
The ribosome will now read the mRNA nucleotide bases 3 at a time (i.e. codons). To ensure the bases are read correctly (to make the correct protein), a reading frame (a particular system for separating a base pair sequence into readable codons) is established at the tRNA-AUG pairing location on the mRNA.

127
Q

Describe translation elongation

A

Step 1: Elongation begins when the initiator tRNA is bound to the P site, the A site is empty
Step 2: The second tRNA with the appropriate anticodon and amino acid binds to the mRNA codon in the A site of the ribosome The 1st amino acid (Met) is cleaved from the tRNA in the P site and forms a peptide bond with the amino acid on the tRNA in the A site. The new polypeptide chain is attached to the tRNA in the A site and the empty tRNA is in the P site
Step 3: The ribosome moves to the next codon on mRNA. tRNA in the A site moves to the P site, tRNA in the P site moves to the E site. The A site becomes open again to accept the next amino acid attached to its tRNA

128
Q

Describe translation termination

A
  • There is no tRNA for the stop codons (UAA, UAG, UGA). When the A site of the ribosome arrives at the stop codon on the mRNA, a protein release factor (RF) binds to this site instead of tRNA.
  • This causes the polypeptide to be released from the P site and it is detached from the ribosome. The ribosomal subunits separate and detach from the mRNA.
  • The polypeptide becomes a functional protein once it goes through some processing and forms its 3D shape. Some proteins are composed of two or more polypeptide chains (e.g., hemoglobin). These polypeptides are produced via separate translation events and come together to form a single functioning protein.
129
Q

What is the lac operon? Is it induction or repression?

A

Enzyme Induction: The lac operon is a cluster of genes that contain the DNA sequences to regulate the protein needed for the metabolism of lactose. The lac operon is known as an inducible operon because the inducer (signal molecule e.g., lactose) inactivates the repressor and allows the gene to be transcribed and translated to produce a protein.

130
Q

What are the 4 components of operons?

A
  1. promotos
  2. operator
  3. coding regions
  4. repressor proteins
131
Q

What is the promotor region?

A

site where transcription occurs/RNA polymerase binds

132
Q

What is the operator region?

A

sequence of bases that regulatory factors will bind to in order to control transcription

133
Q

What are repressor proteins?

A

binds to the operator to repress transcription

134
Q

What happens if lactose is not present in the lac operon?

A
  • lacI protein binds to the operator, covering part of the promoter.
  • RNA Polymerase cannot bind to the promoter
  • Transcription is blocked. Therefore, no mRNA made, no translation occurs = no enzymes made.
135
Q

What happens if lactose is present in the lac operon?

A
  • Lactose binds to lacI protein, changing its shape (induced-fit)
  • lacI can no longer bind to the operator
  • Transcription and translation proceed and the lactose metabolism enzymes are made
136
Q

What is the trp operon? Is it induction or repression?

A

The trp operon is an example of enzyme repression: the operon is repressed (turned off) when high levels of tryptophan are present. Therefore no tryptophan will be produced.

137
Q

What happens if tryptophan is not present in the trp operon?

A
  • Repressor protein is inactive and does not bind to the operator.
  • RNA polymerase binds to the promoter region and transcription occurs.
  • Tryptophan is produced.
138
Q

What happens if tryptophan is present in the trp operon?

A
  • Tryptophan acts as a signal molecule and activates the repressor protein – in this situation, tryptophan is called a corepressor.
  • Tryptophan will bind to the trp repressor, which activates it. The active trp repressor will bind to the operator and stop transcription.
  • No tryptophan is produced.
139
Q

What is a missense mutation?

A

one amino acid is exchanged for another

140
Q

What is a nonsense mutation?

A

a codon for an amino acid is replaced by a stop codon.

141
Q

What is a silent mutation?

A

a mutation that does not change the amino acid coded for, and therefore is no phenotypic change (ex. error in an intron, wobble hypothesis)

142
Q

What is a frameshift mutation?

A

mutation that causes the reading frame of codons to change. Results in different amin acids being incorporated into polypeptide.

143
Q

What are the 4 mutation results?

A

missense, nonsense, silent, and frameshift

144
Q

What are the 4 types of mutations?

A

substitution, insertion, deletion, inversion

145
Q

What is substitution and what mutation does it result in?

A

the replacement of one base with another; results in missense, nonsense, silent

146
Q

What is insertion and what mutation does it result in?

A

the addition of an extra base pair in a DNA sequence; results in a frameshift mutation

147
Q

What is deletion and what type of mutation will it cause?

A

the elimination of a base pair or group of base pairs from DNA sequence; results in frameshift mutation

148
Q

What is inversion and what mutation will it cause?

A

the reversal of 2 adjoining base pairs in a DNA sequence; results in missense mutation

149
Q

What is negative feedback?

A
  • Primary mechanism of homeostasis
  • A stimulus (from change in internal/external environment) triggers a response that will compensate that change to maintain equilibrium
  • Ex: household thermostat – when the room temperature moves away from the desired set point, the integrator circuit in the thermostat activates an electrical effector (either furnace of a/c), which returns the temperature in the room to the set point.
150
Q

What is positive feedback?

A
  • a response of a system that acts to increase the effect of any changes made to the system
  • sets in motion a chain of events that intensify a change from an original condition usually does not result in homeostasis; generally associated with system instability
  • Ex. childbirth: Uterine contractions stimulate the release of oxytocin; Oxytocin increases and intensifies the contractions, which results in more oxytocin to be released and stronger contractions; This positive feedback cycle continues, and eventually leads to the delivery of a baby
151
Q

What is the main difference between positive and negative feedback?

A

Negative feedback stops when the system returns to equilibrium, whereas positive feedback continues until an external limit or intervention halts the process.

152
Q

What is thermoregulation?

A

The maintenance of body temperature within a range that allows cells to function efficiently

153
Q

Describe the body’s response to heat stress

A
  1. thermoreceptors in skin detect rise in body temperature
  2. hypothalamus turns on cooling system
  3. a) sweat glands initiate sweating (evaporation fo sweat causes cooling) b) blood vessels dilate (blood flows to skin and loses heat to skin)
  4. body temperature returns to normal
  5. hypothalamus turns of cooling system
154
Q

Describe the body’s response to cold stress

A
  1. thermoreceptors in skin detect drop in body temperature
  2. hypothalamus turns on warming system
  3. a) arterioles constrict (limits blood flow and reduces heat loss from skin) b) goosebumps (erect hair traps warm air near skin and reduces heat loss) c) shivering (muscle contractions generate heat by increaing metabolism)
  4. body temperature returns to normal
  5. hypothalamus turns off warming system
155
Q

Decribe the process of glomerulus and Bowman’s capsule and the substances transported.

A

Filtration of water and dissolved solutes occurs as blood is forced through walls of glomerulu into Bowman’s capsule by fluid in capillaries. Filtrates include Na+, Cl-, water, H+, glucose, amino acids, vitamins, urea, and uric acid.

156
Q

What are the 3 steps of urine formation?

A
  1. Filtration – movement of fluids from the blood in the glomerulus to the Bowman’s capsule
  2. Reabsorption – transfer of fluids from nephron into peritubular capillaries
  3. Secretion – transfer of fluids from peritubular capillaries into nephron
157
Q

What occurs in filtration of urine formation?

A

(passage of bodily fluids through selectively permeable membrane)
- Occurs in the glomerulus
- Occurs when blood under high pressure (>65mmHg) from the afferent arterioles moves into glomerulus
- High pressure forces water and dissolved solutes (glucose, amino acids, NaCl, H+, vitamins, minerals, urea) through walls of glomerulus and into bowman’s capsule
- Filtration is based on size of molecules; thus, useful molecules also enter the filtrate and must be reabsorbed
- Larger particles (proteins, red blood cells, platelets) are too large to pass through and remain in arteriole blood

158
Q

What occurs in reabsorption in urine formation?

A

(return substances to the blood)
Proximal Tubule
- Lined with cells that contain many mitochondria to power selective reabsorption
- Some substances are reabsorbed by active transport and some by passive transport
- Na+, K+, glucose, and amino acids are actively transported back into the bloodstream (reabsorbed)
- Positive ions carry negatively charged ions with them (like HCO3- and Cl-)
- The pH balance is maintained by the movement of HCO3 - and H+
- Export of solutes out of nephron creates an osmotic gradient that draws water out of the nephron and into interstitial fluid (reabsorption of H2O)
- NH3 and H+ (via ion exchange) are secreted into the tubule to eventually exit as waste
Descending Loop of Henle
- Reabsorption of H2O (filtrate therefore becomes very concentrated)
Ascending Loop of Henle
- Reabsorption of NaCl (made easy by the conc. gradient created in the descending loop)
Distal Tubule
- More selective reabsorption of nutrients
- Further pH maintenance
- Secretion of K+, H+ & ammonia

159
Q

What happens during secretion in urine formation?

A

(movement of wastes/ toxins from the blood back into nephron)
- Remaining filtrate contains some H2O, excess K+ ions, nitrogenous wastes (urea), minerals, salt (NaCl) and other substances (like some drugs)
- Enters the collecting duct
- Collecting ducts merge into the ureter, which empties into the bladder

160
Q

What glands and hormones are involved in the nervous system (brain)?

A
  1. Hypothalamus: neurohormones
  2. Pineal gland
  3. Anterior pituitary gland: FSH (follicle-stimulating), LH (luteinizing), ACTH (adrenocorticotropic), TSH (thyroid-stimulating), Prolaction, Endorphin, GH (growth hormone)
  4. Posterior pituitary gland: oxytocin, ADH (antidiruetic)
161
Q

What glands and hormones are involved in the thyroid?

A
  1. Thyroid gland
  2. Parathyroid gland
162
Q

What glands and hormones are involved in the kidney?

A

(both in the adrenal glands)
1. cortex: epinephrine and norepinephrine (stress)
2. aldosterone and cortisol

163
Q

What is glucagon?

A

produced by pancreas when blood sugar levels are low, converts glycogen to glucose

164
Q

What is insulin?

A

produced by pancreas when blood sugar is high and makes cells more permeable to glucose (negative feedback mechanisms control blood glucose levels by increasing or decreasing insulin)

165
Q

What glands and hormones are involved in the pancreas?

A
  • islets of Langerhans: insulin and glucagon
166
Q

What is the short term response?

A
  • regulated by nervous system
  • adrenal medulla produces epinephrine (adrenaline) and norepinephrine
  • in times of stress epinephrine and norepinephrine are released into blood; prepares the body for a fight-or- flight response
167
Q

What effects does epinephrine have on the short term stress response?

A
  1. glycogen breakdown into glucose -> increases blood sugar level and results in a sudden burst of energy
  2. increases heart rate and respiratory rate and cell metabolism
  3. vasodilation -> increases blood supply oxygen and nutrients to tissues (i.e., muscle)
  4. retinal dilation -> enhanced visual perception
168
Q

What effects does norephinephrine have on the short term stress reponse?

A
  1. has the same effects as epinephrine, also increases blood pressure
  2. affects the amygdala – an attention centre in the brain
169
Q

What are the 4 reproductive hormones?

A
  • estrogen
  • progesterone
  • follicle stimulating hormone (FSH)
  • luteinizing hormones (LH)
170
Q

Where is estrogen produced and when does it peak?

A

ovaries; ovulation

171
Q

Where is progesterone produced and when does it peak?

A

ovaries; luteal phase

172
Q

Where is FSH produced and when does it peak?

A

pituitary gland; ovulation

173
Q

Where is LH produced and when does it peak?

A

pituitary gland; ovulation

174
Q

What are the 4 phases of a woman’s cycle and how long do they last?

A
  • Flow Phase (day 1-5)
  • Follicular Phase (day 6-13)
  • Ovulation (day 14)
  • Luteal Phase (day 15-28)
175
Q

What is population size

A

(Nt): the number of individuals of a specific species that occupies a given area or volume at a given time.

176
Q

What is population density?

A

(D): the number of individuals of the same species that occurs per unit area of volume

177
Q

What is biotic potential?

A

the rate at which species reproduces with unlimited conditions

178
Q

What are the 3 dispersion patterns?

A
  1. clumped
  2. random
  3. uniform
179
Q

What is the clumped dispersion pattern?

A

where individuals are grouped more closely together; this can be due to limited seed dispersal or asexual reproduction.

180
Q

What is the random dispersion pattern?

A

when organisms are distributed independently of each other; this happens when conditions do not vary within a habitat and individuals are neither attracted nor repelled by each other.

181
Q

What is the uniform dispersion pattern?

A

when individuals are more widely separated. Individuals are equally spaced throughout a habitat; this happens when individuals compete for food, breeding or nesting grounds.

182
Q

What are the methods of population growth? (hint: curves)

A
  1. geometric/exponential (J-shaped curve)
  2. sigmoid/logarithmic (S-shaped)
183
Q

What is the geometic/exponential population growth?

A

J shaped curve; organisms reproduce continuously at a constant rate.

Ex: bacteria

184
Q

What is sigmoid/logarithmis population growth?

A

S shaped curve; a type of population growth that starts slow, accelerates/grows rapidly, then levels out over time; the population grows slowly when the population size is small bc few individuals are reproducing; it also grows slowly when the population is large bc it approaches the carrying capacity

185
Q

Define density dependent factors and list the 5 factors.

A

limit the growth of population and are dependant on the population density
1. competition
2. predation
3. crowding
4. allee effect
5. disease and parasites

186
Q

What is competition? (density dependent factors)

A
  • an interaction in which both competing populations lose access to some resources
  • becomes more intense when more individuals are competing for the same resource
    1. interspecific competition: competition between members of different species
    2. intraspecific competition: competition between members of the same population
187
Q

What is predation? (density dependent factor)

A
  • the interaction between predator and prey
  • when one organism kills and eats another, is more competitive when the population density of predators is high
188
Q

What is crowding? (density dependent factor)

A
  • only occurs in high-density population with limited space
  • individuals living in extremely dense population are less likely to survive, they grow slowly and tend to be small
189
Q

What is allee effect? (density dependent factor)

A
  • a phenomenon that occurs when a population cannot survive or fails to reproduce to offset mortality once the population density is too low
  • This effect can produce extinction risk.
190
Q

What is disease and parasites? (density dependent factors)

A
  • Disease is more likely to break out and result in deaths when more individuals are living together in the same place.
  • Parasites are also more likely to spread under these conditions
191
Q

Define density independent factors and list the 2 factors

A

limits the growth of a population regardless of the population density
- Natural disturbances (fires, earthquakes, storms etc)
- Temperature fluctuations

192
Q

What are niches?

A

a population’s niche is defined by the resources it uses and the environment conditions it requires over its lifetime

193
Q

What is a fundamental niche?

A

the range of conditions and resources that a population can possibly tolerate and use

194
Q

What is a realized niche?

A

the range of conditions and resources that a population actually uses in nature

195
Q

What are the 5 defence mechanisms?

A
  1. camouflage
  2. chemical defence
  3. behavioural defence
  4. mimicry (batesian and mullerian)
  5. spines and armour
196
Q

What is camouflage? Give an example.

A
  • an organism mimics the patterns of its environment
  • ex. rockfish use disruptive coloration to hinder detection and to blend into background
197
Q

What is chemical defence? Give an example.

A
  • an organisms is chemical unattractive, either by realsign noxious odious or by concentrating poisonous chemicals in its body
  • ex. skunks produce a noxious chemical
198
Q

What is behavioural defence? Give an example.

A
  • this defence can be passive (hiding, freezing or playing dead) or active (fleeing, herding, mobbing, or using distraction displays)
  • fight and flight
  • ex. rabbits use both freezing and hiding to avoid becoming prey
  • ex. squid and octopuses use ink clouds as a form of display distraction
199
Q

What is batesian mimicry? What is mullerian mimicry? Give an example.

A
  • one species evolves to resemble another
  • Batesian: a harmless species resembles a poisonous one
  • Mullerian: two or more poisonous species that share common predators look the same
  • ex. The viceroy and the monarch butterflies use mullerian mimicry. They are both unpalatable and look very similar
200
Q

What is spines and armour? Give an example.

A
  • various animals and plants have hard, thorny, or needle-like structures
  • ex. porcupine releases hairs that have been modifies ino sharp barbed quills
  • ex. prickly pear cactus use spines for protection.

GRADE 12 (5 decks)

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