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IB Bio > Chapter 2 Understanding & Application > Flashcards

Chapter 2 Understanding & Application Flashcards

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Biology 101 flashcards
1
Q

List types of lipids

A
  • fatty acids
  • steroids
  • triglycerides
  • phospholipids
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2
Q

List types of nucleic acids

A
  • DNA
  • RNA
  • nucleotides
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3
Q

What is anabolism? List examples

A

building up larger molecules
e.g. photosynthesis
converting amino acids into proteins

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4
Q

What is catabolism? List examples

A

breaking down larger molecules
e.g. cell respiration
- glycolysis
- nucleic acids –> nucleotides

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5
Q

Benefit of cohesive property of water

A
  • allows surface tension (insects can glide)
  • creates chain of water molecules (transport through xylem)
  • high heat capacity of water (more energy needed to break these bonds b/w water molecules) –> maintains stable env. for living organisms
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6
Q

Benefit of adhesive property of water

A
  • needed for water to move from roots to leaves - sticks to sides of xylem wall
  • capillary action allows blood to move through vessels
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7
Q

Why is water a good solvent?

A

polarity + H bonding w/ substances

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8
Q

High melting & boiling point of water

A
  • due to H bonds
  • causes water to be liquid in most habitats
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9
Q

High specific heat capacity of water

A
  • amount of heat that must be absorbed/released for 1 g of a substance to change its temp. by 1 C
  • H-bonds
  • protects habitats from lethal temp. fluctuations
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10
Q

High latent heat of vaporisation (coolant)

A
  • amount of heat needed to change 1 g of liquid to a gas
  • H-bonds
  • as water evaporates, surface left behind is cooler
  • allows organisms to cool w/ sweating
  • removes heat from body
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11
Q

What type of bond forms b/w monosaccharides?

A

glycosidic linkages

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12
Q

What type of bond forms b/w amino acids?

A

peptide bonds

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13
Q

What type of bond forms b/w glycerol & fatty acids in lipids?

A

ester linkages

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14
Q

What types of bonds form between nucleotides?

A

phosphodiester bonds

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15
Q

Where do saturated & unsaturated fatty acids originate from?

A
  • saturated = linear, originated from animal source, solid at room temp.
  • unsaturated = bent, originated from plant source (oil), liquid at room temp.
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16
Q

Do trans or cis fatty acids have high melting points?

A

trans have high melting point & are solids at room temp. –> OCCUR IN PROCESSED FOODS

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17
Q

Distinguish b/w fats & oils

A

FATS
- solids at room temp.
- animal sources
- contain more saturated fatty acids
- e.g. butter

OILS
- liquids at room temp
- plant sources
- contain more unsaturated fatty acids
- e.g. olive oil

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18
Q

State functions of triglycerides

A
  • energy
  • storage of energy
  • thermal insulation
  • protection of organs
  • water proofing
  • structural roles (e.g. cholesterol)
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19
Q

Structural difference b/w alpha & beta glucose

A
  • OH is DOWN on C-1 in alpha, but UP on C-1 in beta
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20
Q

Outline the structure & function of cellulose

A
  • forms plant cell wall
  • polymer of Beta glucose
  • linear molecule
  • bound in 1-4 arrangement
  • tensile strength
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21
Q

Outline the structure & function of glycogen

A
  • in animals
  • alpha glucose
  • branched molecule
  • both 1-4 and 1-6 linkages
  • insoluble
  • energy storage
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22
Q

Outline the structure & function of starch in plants

A
  • starch is polymer of a-D-glucose
  • helical shape
    d. storage of glucose/energy in plants
    e. storage form that does not draw water
  1. amylose
    - only 1-4 linkages so unbranched
  2. amylopectin
    - 1-4 AND 1-6 linkages so branched
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23
Q

How many types of amino acids exist?

A

many, but only 20 used in living organisms

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24
Q

How many possible amino acid sequences given n number of amino acids?

A

20^n possible dif amino acid sequences

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25
Q

Distinguish b/w polypeptide & protein

A

when polypeptide folds into specific 3D structure, it is known as protein

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26
Q

Example of protein (structure & function)

A

HEMOGLOBIN
- made of 4 subunits, each having 1 polypeptide chain + 1 heme group
- found in red blood cells that transports oxygen from lungs to tissues

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27
Q

Define globular proteins

A
  • polypeptide chain folds up into a compact shape like a ball w/ an irregular surface
  • e.g. enzymes
  • usually have rounded shape
  • FUNCTIONAL PROTEIN
    e.g. hemoglobin, insulin, catalase
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27
Q

Define globular proteins

A
  • polypeptide chain folds up into a compact shape like a ball w/ an irregular surface
  • e.g. enzymes
  • usually have rounded shape
  • FUNCTIONAL PROTEIN
    e.g. hemoglobin, insulin, catalase
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28
Q

Define fibrous proteins

A
  • simple, elongated 3D shape
  • have roles in cell requiring each individual protein molecule to span large distance
  • STRUCTURAL PROTEIN
  • e.g. collage, myosin, fibrin, actin, keratin
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29
Q

Functions of proteins

A
  • contraction / movement
  • enzyme
  • hormone
  • immune defense
  • pigment
  • receptor
  • storage
  • structure
  • transport
  • catalysis
30
Q

Why does each cell of an organism have unique proteome?

A
  • cells w/ different functions will produce dif. proteins as dif genes are expressed in dif cells
30
Q

Why does each cell of an organism have unique proteome?

A
  • cells w/ different functions will produce dif. proteins as dif genes are expressed in dif cells
31
Q

State the function of rhodopsin

A

a pigment protein found in rod cell of retina
- extremely sensitive to light & thus enables vision in low light conditions

32
Q

State the function of collagen

A
  • structural protein
  • 3 polypeptides wound together to form rope-like conformation
  • used in skin to prevent tearing
  • in bones to prevent fractures
  • in tendons & ligaments for tensile strength
  • the main component of connective tissue
  • most abundant protein in mammals
33
Q

State the function of spider silk

A
  • structural protein
  • used to make webs for catching flies / prey
  • very high tensile strength
  • resists breakage
34
Q

Define denaturation

A

the alteration of a protein shape through some form of external stress (e.g. heat / acid) in such a way that it will no longer be able to carry out its cellular function

35
Q

Outline the effects of heat on protein structure

A
  • disrupts H bonds & non-polar hydrophobic interactions within proteins
  • occurs because heat increases the kinetic energy & causes molecules to vibrate so rapidly & violently that bonds are broken
  • can lead to altered protein recognition or an enzyme might becomes inactive
36
Q

Outline the effects of pH on protein structure

A
  • affect state of ionisation of acidic / basic amino acids
  • if the state of ionisation of amino acids in a protein in altered then the ionic bonds that help to determine 3D shape will be altered
  • leads to protein denaturation
37
Q

List examples of industries in which enzymes are use

A
  • food production
  • food processing
  • food preservation
  • washing powders
  • textile manufacture
  • leather industry
  • paper industry
  • medical applications
38
Q

How & why are industrial enzymes often immobilised?

A
  • resistance to denaturation
  • catalysis can be controlled
  • enzyme concentrations higher
  • products not contaminated w/ enzymes
39
Q

Define immobilised enzyme

A

an enzyme attached to an inert, insoluble material

40
Q

Methods of enzyme immobilisation

A
  • attachment to surface such as glass (ADSORPTION)
  • entrapment in membrane / gel (e.g. alginate)
  • aggregation by bonding enzymes together into particles of up to 0.1 mm diameter
41
Q

State source of lactase enzyme in food processing

A

obtained from yeast - yeast is cultured, lactase is extracted + purified

42
Q

Production of lactose-free milk

A
  • lactase added to milk (may be immobilised on surface or in beads of a porous material)
  • alginate beads containing lactase & putting them into milk
  • lactose concentration drops & glucose concentration rises
43
Q

Advantages of lactose-free milk

A
  • sweeter
  • less crystallisation (more soluble)
  • faster fermentation = yoghurt / cheese
44
Q

What are pyrimidines?

A
  • single ring nitrogenous bases
  • cytosine
  • thymine
  • uracil
45
Q

What are purines?

A
  • double ring nitrogenous bases
  • guanine
  • adenine
46
Q

How many nitrogenous bases per complete turn of DNA double helix?

A

10 pairs of bases per turn

47
Q

Define semi-conservative

A
  • the products of DNA replication each contain one of the ORIGINAL strands & one NEW strand
48
Q

In which direction is the parent strand READ?

A

from 3’ to 5’ direction

49
Q

In which direction is the daughter strand BUILT?

A

from 5’ to 3’ direction
- DNA polymerase adds the 5’ end of the incoming nucleotide to the 3’ end of the previously placed nucleotide

50
Q

Where does transcription occur?

A

in the nucleus

51
Q

Where does translation occur?

A

at a ribosome

52
Q

Outline the genetic code

A
  • rules used by all cells to translate info encoded within genetic material (DNA) into proteins
53
Q

Define redundant in terms of genetic code

A

genetic code is redundant, meaning more than one codon may specify a particular amino acid (means DEGENERATE)

54
Q

Benefits of using gene transfer technology to produce insulin

A
  • biotechnologically produced insulin is indistinguishable from human insulin produced in pancreas
  • large quantities of insulin produced
  • ethical issues eliminated (e.g. can’t use pig insulin)
  • this type of insulin is absorbed more rapidly
55
Q

How many amino acids are in insulin?

A

51

56
Q

Define cell respiration

A

the controlled release of energy from organic compounds to produce ATP

57
Q

Uses of ATP in cell

A
  • powers active transport
  • synthesises polymers
  • moves structures within the cell

ENERGY IS RELEASED WHEN PHOSPHATE GROUP IS REMOVED FROM ATP IN HYDROLYSIS REACTION

58
Q

Compare the total amount of ATP made from anaerobic & aerobic respiration.

A
  • net of 2 ATPs per molecule of glucose (ANAEROBIC)
  • net of 38 ATPs per molecule of glucose (AEROBIC)
59
Q

How is anaerobic respiration in yeast used to make ethanol drinks & biofuel?

A
  • yeast can be used to produce ethanol by fermentation
  • yeast is cultures in liquid containing sugar & other nutrients
  • no oxygen, so respires anaerobically
  • ethanol concentration of fluid around yeast cells rises to ~ 15% by vol
  • fermentation ends, CO2 bubbles out into atm
  • alcohols brewed
  • also ethanol can be used for fuel
60
Q

Which wavelengths of light does chlorophyll absorb?

A

red and blue

61
Q

Define accessory pigments

A

Accessory pigments are light-absorbing compounds, found in photosynthetic organisms, that work in conjunction with chlorophyll a
e.g. chlorophyll b or carotenoids

62
Q

Where does photolysis occur?

A

in thylakoids

63
Q

Define limiting factor

A
  • the variable of a system that can limit the rate of a reaction
    e.g. light, temp. CO2
64
Q

Explain how hydrophobic and hydrophilic properties contribute to the arrangement of molecules in a membrane (7)

A

a. hydrophilic is attracted to/soluble in water and hydrophobic not attracted/insoluble
b. hydrophilic phosphate/head and hydrophobic hydrocarbon/tail in phospholipids
c. phospholipid bilayer in water/in membranes
d. hydrophilic heads «of phospholipids» face outwards/are on surface
e. hydrophobic tails «of phospholipids» face inwards/are inside/are in core
f. cholesterol is «mainly» hydrophobic/amphipathic so is located among phospholipids/in hydrophobic region of membrane
g. some amino acids are hydrophilic and some are hydrophobic
h. hydrophobic «amino acids/regions of» proteins in phospholipid bilayer «core»
i. hydrophilic «amino acids/regions of» proteins are on the membrane surface
j. integral proteins are embedded in membranes due to hydrophobic properties/region
OR transmembrane proteins have a hydrophobic middle region and hydrophilic ends
k. peripheral proteins on are on the membrane surface/among phosphate heads due to being «entirely» hydrophilic OR «carbohydrate» part of glycoproteins is hydrophilic so is outside the membrane
l. pore of channel proteins is hydrophilic

65
Q

What are phosphates used to make?

A

phospholipids/nucleotides/nucleic acids/DNA/RNA/ATP

66
Q

What are nitrates used to make?

A

amino acids/proteins/nucleotides/nucleic acids/DNA/RNA/ATP

67
Q

Outline the importance of water to living organisms

A

a. coolant in sweat/in transpiration;
b. water has a high heat of vaporisation / heat taken when hydrogen bonds break;
c. water is cohesive so can pulled up/so can be moved under tension in xylem;
d. water is an excellent/universal solvent/dissolves many different substances;
e. medium for transport in blood/xylem/phloem;
f. medium for metabolic reactions / (metabolic) reactions happen dissolved in water;
g. surface tension due to cohesion allows organisms to live on water surface;
h. water has high heat capacity so much energy required to change its temperature;
i. ice floats so lakes/oceans do not freeze allowing life under the ice;
j. high heat capacity so stable habitat/so temperature of water changes slowly;
k. used in chemical reactions/photosynthesis/hydrolysis in organisms;

68
Q

To which end are nucleotides added in transcription?

A

added to 3’ end (5’ to 3’ direction)

69
Q

Define condensation

A

joining together molecules with the release of water

70
Q

State the role of four named minerals needed by living organisms.

A

sulfur – part of amino acids / proteins;
calcium – strengthening/formation of bones / muscle contraction / synaptic transmission;
phosphorus – formation of nucleic acids / ATP / GTP / NADP / phospholipids;
iron – formation of hemoglobin / transport of oxygen;
sodium – nerve impulse / sodium-potassium pump / osmoregulation;
potassium – nerve transmission / sodium-potassium pump / osmoregulation;
magnesium – part of chlorophyll molecule;

71
Q

Distinguish b/w fibrous & globular proteins.

A
  • fibrous proteins are strands/sheets whereas globular proteins are rounded;
  • fibrous proteins (usually) insoluble whereas globular proteins (usually) soluble;
  • globular more sensitive to changes in pH/temperature/salt than fibrous;

IB Bio (10 decks)

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