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biology year 12 > topic one > Flashcards

topic one Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what is a monomer

A

small units that can form polymers

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2
Q

what is a polymer

A

large complex molecules made from monomers

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3
Q

what is a condensation reaction

A

joins 2 molecules and involves the release of a water molecule

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4
Q

what is a hydrolysis reaction

A

breaks a chemical bond between 2 molecules and involves the use of a water molecule

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5
Q

3 examples of monosaccharides (carbohydrates)

A

glucose, fructose, galactose

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6
Q

what type of bond does a condensation reaction between 2 monosaccharides form

A

glycosidic bond

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7
Q

what is maltose made from

A

glucose + glucose

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8
Q

what is sucrose made from

A

glucose + fructose

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9
Q

what is lactose made from

A

glucose + galactose

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10
Q

what type of glucose do starch and glycogen use

A

alpha glucose

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11
Q

what type of glucose does cellulose use

A

beta glucose

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12
Q

structure and function of starch

A

helical structure makes it compact = good for storage
insoluble, doesn’t affect water potential = good for storage
- long and branched chain

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13
Q

structure and function of glycogen

A

helix makes it compact = good for storage
insoluble, doesn’t affect water potential = good for storage
branched means glucose can be released quick for respiration

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14
Q

structure and function of cellulose

A

hydrogen bonds ensure microfibrils are strong, gives strength to cell wall = prevents cell from bursting when water enters by osmosis
- long and unbranched

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15
Q

test for protein

A

add water and shake, then add 3/4 drops of biuret
positive result = lilac

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16
Q

test for reducing sugar

A

add water and equal amount of benedict’s, heat for 5 mins
positive result = brick red

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17
Q

test for non reducing sugar

A

carry out reducing sugars test (get negative result) take second sample and add water, add dilute HCl and heat for 5 min. add sodium carbonate to neutralise, then re test by adding benedict’s and heating
positive result = lots of colour change, brick red in end

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18
Q

test for starch

A

one/two drops of iodine
positive result = blue black

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19
Q

test for lipids

A

add ethanol and shake, then make a new test tube that contains just water and pour first tube into that
positive result = milky emulsion

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20
Q

how does a triglyceride form

A

condensation reaction between of 1 molecule of glycerol 3 molecules of fatty acids

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21
Q

what bond forms between a fatty acid and glycerol

A

ester bond

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22
Q

what is the difference between saturated and unsaturated fats

A

saturated = no carbon-carbon double bond
monounsaturated = 1 carbon-carbon double bond
polyunsaturated = many carbon-carbon double bonds

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23
Q

what is a phospholipid made from

A

2 fatty acids, 1 glycerol and 1 phosphate

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24
Q

triglyceride structure and properties

A
  • insoluble, good for storage because it doesn’t affect osmosis in cells
  • low mass: energy = good for storage
    fatty acid tail contains a lot of energy, used as energy storage molecules
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25
Q

phospholipid structure and properties

A
  • forms bi-layer within cell surface membrane
  • hydrophilic head/hydrophobic tail form a double layer with heads facing out towards water on either side
    -centre of bi layer is hydrophobic, so water-soluble substances cant pass easily - membrane acts as a barrier
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26
Q

monomer of proteins

A

amino acids

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27
Q

how are dipeptides AND polypeptides formed

A
  • dipeptide = formed when 2 amino acids are joined together
  • polypeptide = formed when more than 2 amino acids are joined
    proteins are made up of one or more polypeptides
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28
Q

amino acid structure (drawing)

A

H H O
I I II
N - C - C
I I I
H H H

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29
Q

general structure of an amino acid

A

carboxyl group, amino group, R group, hydrogen atoms
their R group is what makes them different

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30
Q

what reaction links amino acids

A

condensation

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31
Q

what are the bonds between amino acids called

A

peptide bonds

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32
Q

what reaction happens when di/polypeptides are broken down

A

hydrolysis

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33
Q

primary protein structure

A

the sequence of amino acids in the polypeptide chain

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34
Q

secondary protein structure

A
  • hydrogen bonds form between the amino acids in the chain
  • this makes it coil into an alpha helix or a beat pleated sheet
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35
Q

tertiary protein structure

A
  • the coil/folded chain is coiled/folded further
    -more hydrogen and ionic bonds form between different parts in the chain
    -disulfide bridges also form when two molecules of the amino acid cysteine come close together
36
Q

quaternary protein structure

A
  • the way polypeptide chains are assembled
  • proteins made from more than 1 polypeptide chain, the quaternary structure is the proteins final 3D structure
37
Q

globular proteins example

A
  • haemoglobin
  • enzymes
38
Q

what are globular proteins for

A

metabolism, transport

39
Q

globular proteins structure and function

A
  • hydrophilic r group on the surface makes them soluble in water
40
Q

fibrous proteins example

A
  • keratin
  • collagen
41
Q

what are fibrous proteins for

A

structure

42
Q

fibrous proteins structure and function

A

polypeptide chains lay parallel with cross links make them strong

43
Q

what are enzymes

A

globular proteins which act as biological catalysts that speed up chemical reactions without being altered themselves or used up

44
Q

suffix for most enzymes & which are excluded

A
  • most end in ‘ase’
  • pepsin and trypsin excluded
45
Q

difference between the lock & key model and the induced fit model

A

induced fit model suggests that the substrate and active site aren’t perfectly complementary at first, and the active site has to slightly change shape to bind to the substrate
whereas the lock and key model suggests the active site and substrate are always perfectly complementary

46
Q

factors that affect the rate of reaction

A
  • pH
  • temperature
  • enzyme concentration
  • substrate concentration
  • presence of an inhibitor
47
Q

how does optimum temperature affect rate

A

at optimum temperature, there is more kinetic energy and a higher frequency of collisions between active sites and substrates - therefore more enzyme substrate complexes formed

48
Q

how does high or low temp affect rate

A
  • if the temp is too low, it is too cold for enzymes to function, and therefore fewer particle collisions = slower rate of reaction
  • if the temp is too high, the enzyme will be denatured, hydrogen bonds between amino acids break, and change the shape of the active site = loses function
49
Q

how does enzyme concentration affect rate

A

increase in enzyme concentration will increase the rate until all active sites become saturated

50
Q

what happens if the amount of substrate is limited

A

enzyme concentration will stop increasing

51
Q

how does substrate concentration affect rate

A

increase in rate until all sites are saturated

52
Q

how does pH affect rate

A
  • above or below optimum, hydrogen/ionic bonds will break and alter the shape of the active site
  • enzyme substrate complexes formed less easily
53
Q

what is a competitive inhibitor

A

shape is similar to a substrate and can occupy the active site, may compete for AS with substrate

54
Q

what is a non competitive inhibitor

A

the inhibitor attaches to a binding site which is not the active site, changes shape of enzyme. this means the active site can no longer attach to the substrate = loses function

55
Q

what do DNA/RNA stand for

A
  • deoxyribonucleic acid (DNA)
  • ribonucleic acid (RNA)
56
Q

what are DNA and RNA polymers of

A

nucleotides

57
Q

what are the components of DNA

A
  • pentose sugar
  • phosphate
  • a nitrogen base (adenine, thymine, cytosine, guanine)
58
Q

what forms the backbone of DNA

A

sugar + phosphate

59
Q

structure of DNA

A

double helix with two polynucleotide chains held together

60
Q

physical structure

structure of RNA

A

single strand, short polynucleotide chain

61
Q

what holds the base pairs together

A

weak hydrogen bonds

62
Q

how many bonds between A + T

A

2 hydrogen bonds

63
Q

how many bonds between C + G

A

3 hydrogen bonds

64
Q

which bases are purines and how many rings are the structures

A
  • A + T
  • 2 ring structures
65
Q

what are C + T called and how many rings are the structures

A
  • pyrimidine
  • 1 ring structure
66
Q

what is the bond between 2 nucleotides called

A

phosphodiester bond (condensation reaction)

67
Q

components of RNA

A
  • adenine
  • cytosine
  • guanine
  • uracil
68
Q

why does DNA need to replicate

A

growth and repair

69
Q

what phase does DNA replication take place in

A

S phase

70
Q

what is the difference between the conservative model and the semi-conservative model

A
  • conservative model = parent and daughter DNA kept completely separate
  • semi-conservative model = half its own DNA, half original parent DNA
71
Q

what does ATP stand for

A

adenosine triphosphate

72
Q

what is ATP made from

A

ribose, adenine and 3 phosphate groups

73
Q

how is energy released from ATP

A

energy is released when ATP is hydrolysed to form ADP and inorganic phosphate group. this process is catalysed by ATP hydrolase.

74
Q

where does the energy come from in ATP

A

the bonds between phosphate molecules.

75
Q

what does the condensation of ADP and Pi produce

A

ATP, during respiration and photosynthesis

76
Q

properties of ATP

A
  • it is an immediate source of energy
  • it isn’t stored in large quantities and can easily be reformed back into ADP
  • it is used in many different ways, such as metabolic reactions, active transport and movement.
77
Q

how is ATP re-synthesised

A

the condensation of ADP and Pi
this reaction is catalysed by using ATP synthase

78
Q

why is water polar

A

one end of the molecule is more positive and the other end is more negative

79
Q

how is water a metabolite

A

involved in condensation and hydrolysis, which are used in forming and breaking chemical bonds

80
Q

how is water a solvent

A

it allows gases to diffuse, as well as enzymes and waste products; urea and ammonia

81
Q

why does water have a high specific heat capacity

A

alot of energy is required to break the hydrogen bonds

82
Q

why does water have a high latent heat of vaporisation

A

the hydrogen bonding means a lot of heat is required to evaporate one gram of water.
this means the evaporation of water provides a cooling effect with little water loss.

83
Q

why is strong cohesion between water molecules beneficial

A

between molecules enables transport. it supports columns of water and results in surface tension at the water-air boundary

84
Q

what do hydrogen ions do

A

determine pH of substances such as blood.
higher conc of hydrogen ions = lower pH

85
Q

what are iron ions components of

A

these are a component of haemoglobin and carry oxygen in red blood cells.

86
Q

what are sodium ions involved in

A

involved in co transport of glucose and amino acids

87
Q

what are phosphate ions components of

A

DNA and RNA

biology year 12 (5 decks)

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