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Biology Paper 1 Summary > Topic 1 > Flashcards

Topic 1 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what are monomers

A

smaller units from which larger molecules are made

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2
Q

what are polymers

A

molecules made from a large number of monomers joined together

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2
Q

examples of monomers

A

nucleotides
amino acids
monosaccharides

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3
Q

examples of polymers

A

DNA/RNA
protein
polysaccharides

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4
Q

whats a condensation reaction

A

the joining of two molecules forming a chemical bond with the removal of a water molecule

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5
Q

whats a hydrolysis reaction

A

breaking of a chemical bond between two molecules using a molecule of water

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6
Q

what are monosaccharides

A

monomers from which larger carbs are made

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7
Q

examples of monosaccharides

A

glucose galactose and fructose

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8
Q

what type of bond forms when a condensation reaction occurs between two monosaccharides

A

a glycosidic bond

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9
Q

a condensation reaction between two glucose molecules forms..

A

maltose

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9
Q

what is a disaccharide

A

two monosaccharides joined by a glycosidic bond

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10
Q

sucrose is formed from..

A

a glucose and fructose molecule

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11
Q

glucose + galactose =

A

lactose

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12
Q

what are the three types of glucose

A

starch, cellulose and glycogen

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13
Q

what are the two types of starch

A

amylose and amylopectin

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14
Q

what monomer of glucose is starch made from

A

alpha glucose

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15
Q

what is the function of starch

A

to store glucpse

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16
Q

where is starch usually found

A

in plants

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17
Q

describe the glycosidic bonds in amylose

A

1-4

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18
Q

describe the glycosidic bonds in amylopectin

A

1-4 and 1-6

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19
Q

describe the structure of amylose

A

alpha coiled helix structure

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20
Q

how does the structure of amylose relate to its function

A

coiled helix allows for compactness which allows for lots of glucose to be stored

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21
Q

what is the structure of amylopectin

A

branched molecule

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22
Q

how does the structure of amylopectin relate to its function

A

branches allow for larger surface area so rapid hydrolysis is enabled

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23
Q

which glucose monomer makes up cellulose

A

beta glucose

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24
Q

where is cellulose found

A

plants - cell walls

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25
Q

what is the function of cellulose

A

to provide structural support

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26
Q

describe the glycosidic bonds in cellulose

A

1-4

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27
Q

what is the structure of cellulose

A

straight branched chains with hydrogen bonds between them to form fibrils

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28
Q

how are fibrils formed

A

hydrogen bonds between straight chains

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29
Q

how does the structure of cellulose relate to its function

A

lots of hydrogen bonds allows for strength

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30
Q

what monomer of glucose makes up glycogen

A

alpha

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31
Q

describe the glycosidic bonds in glycogen

A

1-4, 1-6

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32
Q

where is glycogen found

A

animals

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33
Q

what is the function of glycogen

A

stores glucose

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34
Q

describe the strucutre of glycogen

A

highly branchedh

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35
Q

how does the structure of glycogen relate to its function

A

lots of branches allows for rapid hydrolysis of the molecule and effective release of glucose

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36
Q

what are the two types of lipids

A

triglycerides and phospholipids

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37
Q

describe the structure of a triglyceride

A

one glycerol molecule with 3 fatty acids

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38
Q

describe the structure of a phospholipid

A

a glycerol molecule with 2 fatty acids and one phosphate group attached

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39
Q

what type of reaction occurs between the glycerol and fatty acids to form a triglyceride/phospholipid

A

condensation reaction

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40
Q

what is the bond between a glycerol and fatty acid called

A

ester bond

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41
Q

what does it mean if a fatty acid is saturated

A

there are only single C-C bonds in the hydrocarbon chain

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42
Q

what does it mean if the fatty acid is unsaturated

A

there is at least one C=C in the hydrocarbon chain

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43
Q

why is a lot of energy stored in a triglyceride molecule

A

theres a large ratio of emergy storing carbon-hydrogen bonds compared to the number of carbon atoms > lots of energy is stored in the molecule

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44
Q

why are triglycerides a metabolic water source

A

high ratio of hydrogen to oxygen atoms so they can release water if oxidised

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45
Q

why do triglycerides not affect osmosis / water potential

A

they are large and hydrophobic > so insoluble in water

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46
Q

what is the effect of lipids having a relatively low mass

A

lots can be stored without increasing the mass and preventing movement

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47
Q

why does a phospholipid have a hydrophilic head

A

negative charge on the phosphate group > attracts water and repels fats

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48
Q

why does the fatty acid tail repel water

A

because it is not charged

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49
Q

what is the function of phospholipids

A

to form the phospholipid bilayer

50
Q

how does the structure of a phospholipids help relate to its function

A

hydrophilic head > faces the water
hydrophobic tails > face eachother

51
Q

from which monomers are proteins made

A

amino acids are the monomers from which proteins are made

52
Q

describe the general structure of an amino acid

A

amine group - NH2
carboxyl group - COOH
central carbon with H and variable group

53
Q

which bond forms when a condensation reaction occurs between two amino acids

A

peptide bonds

54
Q

how are dipeptides formed

A

condensation reaction between two amino acids

55
Q

how are polypeptide formed

A

condensation reaction of many amino acids

56
Q

what are the levels of structure in a protein

A

primary
secondary
tertiary
quaternary

57
Q

describe the primary structure

A

order of amino acids in polypeptide chain

58
Q

describe the secondary structure of a protein

A

sequence of amino acids determines whether the protein bends into an alpha helix or beta pleated sheet
- held together by hydrogen bonds

59
Q

describe the tertiary structure of a protein

A

secondary protein structure is further folded
- hydrogen, ionic and disulfide bridges are formed to hold the structure together

60
Q

describe the quaternary structure of a protein

A

a protein made up of more than one polypeptide chain

61
Q

what is the protein structure level of an enzyme

A

tertiary

62
Q

how does the tertiary structure of an enzyme relate to its function

A

tertiary structure of protein allows for the unique and specific shape of the active site > so enzymes can only attach to complementary substrates

63
Q

what is the function of an enzyme

A

to lower activation energy of reactions they catalyse

64
Q

explain what the induced fit model states

A

the enzyme active site slightly changes shape and moulds around the substrate > causes strain on the bonds allowing for activation energy to be lowered

65
Q

what are the factors affecting enzymes

A

temperature
pH
inhibitors
enzyme conc
substrate conc

66
Q

how does a too low temperature affect enzyme activity

A

not enough kinetic energy for successful collisions between enzyme and substrates

67
Q

what is the affect of a temperature being above the optimum on enzyme activity

A

enzymes active site will denature and change shapes so the substrates will no longer be complementary

68
Q

how does a too low/high pH affect enzyme activity

A

the pH will interfere with the charges in the amino acids in the active site and cause bonds to break causing denaturing of the active site so substrates will no longer be complementary to the active site

69
Q

what is the effect of insufficient substrate on enzyme activity

A

fewer collisions between enzyme and substrate so rare of reaction decreases

70
Q

what is the effect of excessive amounts of substrates on enzyme activity

A

rate of reaction remains constant because theres not enough empty enzyme active sites for substrates to bind to

71
Q

what is the effect of insufficient enzymes on enzyme activity

A

enzyme active sites become saturated with substrate and unable to work any faster

72
Q

what is the effect of too many enzymes on enzyme activity

A

there isnt enough substrate to bind with the enzymes so rate will remain constant

73
Q

what are the two types of inhibitors

A

competitive and non-competitive

74
Q

where do competitive inhibitors bind

A

to the active site

75
Q

why do competitive inhibitors affect enzyme activity

A

they prevent enzyme-substrate complexes

76
Q

how can the effect of competitive inhibitors be counteracted

A

by adding more substrates so that the inhibitors can be knocked out

77
Q

where do non-competitive inhibitors bind

A

not to the active site > allosteric site

78
Q

explain how non-competitive inhibitors effect enzyme activity

A

they bind to the allosteric site which means that the active site shape changes so the substrate is no longer complementary to it so enzyme-substrate complexes cant be formned

79
Q

what is the effect of adding lots of substrate to a reaction with an enzyme with a non-competitive inhibitor

A

no effect > substrate can no longer bind due to changed shape of active site

80
Q

describe the test for starch

A

add iodine dissolved in potassium iodide

81
Q

whats the observation for a positive test for presense of starch

A

orange/brown > blue/black

82
Q

describe the test for reducing sugars

A

add Benedicts reagetn and heat

83
Q

whats the observation for a positive test result of a reducing sugar

A

blue > green, yellow, orange or black

84
Q

how can you determine the concentration of the reducing sugar if present

A

the redder the colour change, the higher the conc

85
Q

describe the test for non-reducing sugars

A

if test for reducing sugars = negative (stays blue)
- add acid and boil (acid hydrolysis)
- cool and neutralise with alkali (sodium hydrogencarbonate)
- add Benedicts and heat

86
Q

what is the observation for a positive result for presence of a non-reducing sugar

A

blue > orange/brick red

87
Q

describe the test for proteins

A

add Biuret to sample

88
Q

what is the observation for a positive test for proteins

A

blue > purple

89
Q

describe the test for lipids

A

dissolve sample in ethaol and shake and add dsitilled water

90
Q

what is the observation of a positive result for the prescence of lipids

A

milky emulsion forms

91
Q

what is the function of DNA

A

codes for the sequence of amino acids in the primary structure of a protein

92
Q

what is the monomer of DNA

A

DNA nucleotides

93
Q

what is the structure of a DNA nucleotide

A

deoxyribose (pentose sugar), nitrogenous base, and one phosphate group

94
Q

what are the nitrogenous bases for DNA

A

guanine, thymine, cytosine and adenine

95
Q

what is the polymer of nucleotides called

A

polynucleotides

96
Q

how are polynucleotides formed

A

condensarion reactions between nucleotides

97
Q

what is the bond between nucleotides called when a condensation reaction occurs

A

phosphodiester bond

98
Q

between what two parts of the nucleotides do phosphediester bonds form

A

the deoxyribose sugar and the phosphate group

99
Q

how is the sugar phosphate backbone

A

condensation reactions between phosphate group and deoxyribose pentose sugar, forming phosphodiester bonds which are very strong

100
Q

structure of RNA nucleotides

A

ribose sugar, phosphate group and nitrogenous bases

101
Q

what are the nitrogenous bases for RNA nucleotides

A

guanine, thymine, cytosine and uracil

102
Q

what are the key differences between RNA and DNA nucleotides

A

DNA:
- double stranded, ATCG, deoxyribose
RNA:
- single stranded, AUCG, ribose and shorter

103
Q

what is the function of RNA

A

to transfer genetic code from DNA in the nucleus to the ribosomes

104
Q

outline the steps of semi-conservative replication

A
  1. DNA Helicase breaks the hydrogen bonds between the complementary base pairs within the double helix
  2. Free DNA nucleotides match up to the complementary base pairs on the two template strands
  3. Condensation reactions occurs between the adjacent nucleotides to form phosphodiester bonds - catalysed by DNA Polymerase
  4. Two sets of daughter DNA contain one of the template strands and one newly synthesised strand
105
Q

what evidence is there for semi-conservative replication

A

Mehelston and Stahl conducted experiments

106
Q

what is ATP

A

adenosine triphosphate

107
Q

describe the structure of ATP

A

adenine, ribose sugar and three phosphate groups

108
Q

what is the function of ATP

A

to provide an immediate source of energy for metabolic processes

109
Q

how is ATP made

A

condensation reaction between ADP and Pi during respiration using enzyme ATP synthase

110
Q

how is energy released from ATP

A

it is hydroylsed into ADP + PI using ATP hydrolase

111
Q

what is phosphorylation

A

when the Pi released during hydrolysis of ATP is bonded onto different compounds to make them more reactive

112
Q

give an example of phosphorylation

A

glucose at the start of respiration

113
Q

what type of bond forms between water molecules and where do they form

A

hydrogen bonds between the oxygen of one molecule and the hydrogen of another

114
Q

why is water considered dipolar

A

hydrogen is slightly positive whilst the oxygen is slightly negative

115
Q

what are the 5 properties of water

A
  1. metabolite
  2. solvent
  3. high specific heat capacity
  4. cohesion
  5. strong latent heat of vaporisation
116
Q

explain why water is a metabolite

A

it is involved in reactions e.g. condensation, hydrolysis

117
Q

explain why water is a good/important solvent

A

it is dipolar > can dissolve solutes and transport them

118
Q

why is it a good thing that water has a high heat capacity

A

our bodys are mainly water, and it takes alot of energy to change the temperature of our bodys and therefore enables enzymes to not be denatured

119
Q

advantage of large latent heat of vaporisation of water

A

provides a cooling effect when we sweat with loss of watter through evaporation

120
Q

how is the cohesion property of water beneficial

A

enables for water columns and provides surface tension > transpiration stream

121
Q

where do inorganic ions occur

A

in solution > cytoplasm and body fluids of organisms

122
Q

whats the role of hydrogen ions

A

lower pH of solutions
impact enzyme function
haemoglobin function

123
Q

role of iron ions

A

component of haemoglobin in the transport of oxygen

124
Q

role of sodium ions

A

co transport of glucose and amino acids in absorption

125
Q

role of phosphate ions

A

component of DNA > phosphodiester bonds
ATP > makes ADP more reactive

Biology Paper 1 Summary (4 decks)

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