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Biology > 3.1 Biological molecules - carbs, proteins, enzymes, lipids and biochemical tests > Flashcards

3.1 Biological molecules - carbs, proteins, enzymes, lipids and biochemical tests Flashcards

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1
Q

what are carbohydrates used by and what for

A

by cells for respiration and as structural components in membranes and cell walls, storage ( starch and glycogen )

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2
Q

what are carbohydrates used by and what for

A

by cells for respiration and as structural components in membranes and cell walls, storage ( starch and glycogen )

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3
Q

what are lipids used for?

A

used for respiration, the bilayer of plasma membranes, some hormones

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4
Q

what are proteins used for?

A

many cell structures, enzymes, chemical messengers, transport and components of the blood

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5
Q

what is water used for?

A

solvent found as the major component of all cells

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6
Q

examples of nucleic acids

A

DNA and RNA

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7
Q

what do nucleic acids do?

A

carry the genetic code for the production of proteins, RNA is part of ribosome structure

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8
Q

what are vitamins and minerals required for?

A

a range of enzyme functions

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9
Q

what is a polymer?

A

a long chain molecule made up of large numbers of repeating units linked together e.g. starch, proteins, DNA

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10
Q

what is a monomer?

A

one of the molecules linked together in the chain to form a polymer e.g. glucose, amino acids, nucleotides

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11
Q

what do 2 monomers make?

A

dimer

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12
Q

what do 3 monomers make?

A

trimer

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13
Q

glucose formula

A

C6H12O6

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14
Q

glucose + glucose

A

maltose + water

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15
Q

what is produced when 2 biological monomers are linked together

A

water

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16
Q

what is the reaction called when 2 biological monomers are linked together and water is produced

A

condensation reaction

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17
Q

what happens to the water molecule in a condensation reaction

A

involve the removal of a water molecule

the removal of water from monomers enables a chemical bond to form between the monomers

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18
Q

what happens during a hydrolysis reaction

A

a water molecule is added between two bonded monomers ( within a dimer or polymer ) to break the chemical bond

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19
Q

what is a hydrolysis reaction?

A

the opposite of a condensation reaction where water is split

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20
Q

what does a condensation reaction involve the removal of?

A

the removal of a water molecule

this removal of water from monomers enables a chemical bond to form between the monomers

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21
Q

what is a hydrolysis reaction?

A

the opposite of a condensation reaction

a water molecule is added between the two bonded monomers to break the chemical bond

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22
Q

what do carbohydrates do?

A

store energy and can provide structural support to plant cells

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23
Q

which carbohydrates are monosaccharides?

A

glucose

fructose

galactose

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24
Q

which carbohydrates are disaccharides?

A

maltose

sucrose

lactose

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25
Q

which carbohydrates are polysaccharides?

A

starch

glycogen

cellulose

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26
Q

what is the general formula for a monosaccharide?

A

CnH2nOn

where n = the number of carbon atoms it contains

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27
Q

what is the formula for glucose?

A

C6H12O6

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28
Q

what is an isomer?

A

compounds that have the same formula but the atoms are arranged differently

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29
Q

what are the structural isomers of glucose?

A

beta glucose and alpha glucose

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30
Q

what are the difference between the structures of alpha and beta glucose?

A

the H group and the OH group on carbon 1 swap position

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31
Q

where are the H group and OH group on carbon 1 on alpha glucose?

A

H group is above and the OH group is below carbon 1

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32
Q

where are the H group and OH group on carbon 1 on beta glucose?

A

H group is below and the OH group is above carbon 1

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33
Q

what is a disaccharide?

A

two monosaccharides bonded together by a glycosidic bond, that is formed by a condensation reaction

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34
Q

glucose + glucose

A

maltose

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35
Q

glucose + galactose

A

lactose

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36
Q

glucose + fructose

A

sucrose

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37
Q

how does a condensation reaction create a disaccharide?

A

a water molecule is removed from the OH group on carbon 1 and carbon 4 on the two monosaccharides

the bond that forms is known as a glycosidic bond

will be a 1-4 glycosidic bond if between carbon 1 and carbon 4

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38
Q

what reaction takes place to make a disaccharide go back to a monosaccharide?

A

hydrolysis reaction

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39
Q

what are polysaccharides?

A

polymers made up of many monosaccharides

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40
Q

how are polysaccharides created?

A

through condensation reactions

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41
Q

where is starch found?

A

plants

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42
Q

what is starch made from?

A

the excess glucose created during photosynthesis

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43
Q

what type of glucose makes up starch?

A

alpha glucose

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44
Q

what type of glycosidic bonds keep starch held together?

A

1,4 and 1,6 glycosidic bonds

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45
Q

what two polymers make up starch?

A

amylose and amylopectin

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46
Q

in starch what do the 1,4 glycosidic bonds in amylose cause?

A

a spiral shaped polymer

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47
Q

in starch what do the 1,4 and 1,6 glycosidic bonds in amylopectin cause?

A

result in branches

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48
Q

is starch soluble or insoluble?

A

insoluble due to the fact it is a large molecule

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49
Q

what is starch being insoluble an advantage?

A

it means it can be stored within cells and not dissolve therefore it will not change the water potential of the cell nor cause osmosis to occur

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50
Q

why is amylose being spiral shaped an advantage?

A

it can be readily compacted

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51
Q

why is amylopectin being branched an advantage?

A

it provides a larger surface area for enzymes to attach to meaning starch is readily hydrolysed back into glucose when plant cells are running low on glucose for respiration

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52
Q

what is glycogen?

A

the major carbohydrate storage molecule found in animal cells

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53
Q

where are the main glycogen cells stored?

A

in the liver and muscle cells

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54
Q

what is glycogen made from?

A

the excess glucose that has been eaten and absorbed into the bloodstream

55
Q

why is glycogen mainly stored in the liver and muscle cells?

A

to ensure they always have access to glucose to respire and release energy

56
Q

what type of glucose is glycogen made up of?

A

alpha glucose

57
Q

why does glycogen have more of a branched structure than amylopectin?

A

because it contains more 1,6 glycosidic bonds

58
Q

is glycogen soluble or insoluble?

A

its insoluble due to the fact its a large molecule

59
Q

why is glycogen being insoluble an advantage?

A

means it can be stored within cells and not dissolve

therefore it will not change the water potential of the cell nor cause osmosis which would cause cell lysis

60
Q

why is glycogen being highly branched an advantage?

A

means it has a larger surface areas for enzymes to attach which means it can be readily hydrolysed into glucose

glycogen is more branched than starch so it can be hydrolysed back into glucose more rapidly

61
Q

why is glycogen being more branched than starch essential for animals?

A

because hey have a higher metabolic rate and therefore need more glucose than plants e.g. running away from a predator

62
Q

what is the function of cellulose?

A

to provide structural strength in plants

63
Q

where is cellulose located in plants and why?

A

in the cell wall of plants and therefore prevents cells from bursting if they take in excess water

64
Q

what type of glucose is cellulose made from?

A

beta glucose

65
Q

what glycosidic bonds is cellulose made up of?

A

1,4 glycosidic bonds only

66
Q

why is the cellulose polymer unbranched?

A

because it is only made up of one type of glycosidic bond

1,4 create straight lines whereas 1,6 create branches

67
Q

what is the structure of cellulose like?

A

the long straight chains of b glucose accumulate and lie parallel to each other

the parallel chains are then held together by many hydrogen bonds which provide strength due to the amount of them

68
Q

what is the structure of cellulose called?

A

fibril

69
Q

is cellulose soluble or insoluble?

A

insoluble

70
Q

why is cellulose being insoluble an advantage?

A

it will not change the water potential of the cell and affect osmosis

71
Q

how is cellulose a very strong polysaccharide?

A

due to the large number of hydrogen bonds in and between the fibrils

72
Q

what is the method of the reducing sugars test?

A
  1. add benedicts reagent to the sample you re testing
  2. heat e.g. using water bath
  3. if a colour change of blue to yellow/ green / ed is observed then it is confirmation that a reducing sugar is present
  4. if the solution remains blue, there is no reducing sugar present
73
Q

what is an example of a non reducing sugar?

A

sucrose

74
Q

why is sucrose not a reducing sugar?

A

because it cannot reduce Cu2+

75
Q

how can we prove that sucrose is still a sugar but is just unable to reduce Cu2+?

A

the glycosidic bond must be hydrolysed to expose the reducing group

76
Q

what is the method for the non - reducing sugar test?

A
  1. mix sucrose with hydrochloric acid and boil
  2. cool the solution and then add sodium hydroxide to make the solution alkaline
  3. add a few drops of benedicts reagent and heat - if a colour change of blue to yellow, green or red is observed then this is confirmation a non reducing sugar is present.
77
Q

why do we mix the sucrose with the HCl and boiled in the non reducing sugars test?

A

this is acid hydrolysis and it breaks the glycosidic bond so that sucrose is hydrolysed back into glucose and fructose

78
Q

why in the non reducing sugars test must we cool the solution and add sodium hydroxide to make it alkaline?

A

cooling is to prevent excessive, dangerous fizzing

the sodium hydroxide is because benedicts only works in alkaline solutions so this stage is essential

79
Q

what does the rustier the red after the reducing or non reducing sugars test mean?

A

the higher the concentration of sugar present because more copper oxide has been made (rust)

80
Q

what is the method for the test for starch?

A

add a few drops of iodine

it will turn blue/black if starch is present

81
Q

what is the method for a test for proteins?

A

add biuret reagent

it will turn from blue to purple if protein is present

82
Q

what is the method for a test for lipids?

A

your sample must first be dissolved in ethanol e.g. by shaking your sample you are testing in ethanol

once the sample is dissolved add distilled water and shake again

if lipids are present, you will observe a white emulsion

83
Q

are proteins polymers or monomers?

A

polymers

84
Q

what monomers are proteins made up of?

A

amino acids

85
Q

what does the general structure of an amino acid include?

A

a central carbon

an amine group (NH2)

a hydrogen atom

a carboxyl group (COOH)

the variable group (R group)

86
Q

what reaction allows amino acids to join together to make the polypeptide polymer?

A

Amino acids join together to make the polypeptide polymer via condensation reactions

87
Q

what bonds keep amino acids together to make polypeptide polymers?

A

peptide bonds

88
Q

what is the first structure that forms in the creation of a protein?

A

the polypeptide chain

89
Q

what is the primary structure of a protein?

A

the primary structure is the sequence of amino acids in a polypeptide chain

90
Q

when will the specific order of amino acids alter?

A

where bonds occur and how the protein folds

91
Q

what does the primary structure determine overall due to the sequence of amino acids?

A

the primary structure determines the final 3D shape and the protein’s function

92
Q

in the secondary structure of a protein what does the sequence of amino acids cause?

A

causes parts of a protein molecule to bend into an α helix or fold into β pleated sheets

93
Q

what bonds form between the carboxyl groups of one amino acid and the amine group of another in the secondary structure?

A

hydrogen bonds which hold the secondary structure in place

94
Q

what bonds hold the tertiary structure together?

A

hydrogen, ionic and disulfide bonds hold the tertiary structure

95
Q

where do disulphide bonds form between in the tertiary structure of a protein?

A

only form between the R-groups of two amino acids that contain sulfur

96
Q

describe the tertiary structure of a protein (3 marks)

A
  • the further folding of the secondary structure
  • to create a unique 3D structure
  • held in place by hydrogen, ionic and disulfide bonds
97
Q

what type of protein has a quaternary structure?

A

a protein that is made up of more than one polypeptide chain has a quaternary structure

98
Q

what is a prosthetic group in the quaternary structure of a protein?

A

any group that is attached to a protein, but is not made up of amino acids

99
Q

why is the active site specific and unique in shape?

A

due to the specific folding and bonding in the tertiary structure of the protein

due to this specific active site, enzymes can only attach to substrates that are complementary in shape

100
Q

where are protein polymer chains, or polypeptides created?

A

on ribosomes in cells and are then further folded and modified in
the Golgi apparatus

101
Q

what do enzymes do to the activation energy?

A

they can lower the activation energy needed for the reaction to occur, and therefore speed up the reaction

102
Q

what is the lock and key model and what does it suggest?

A

this model suggests that the enzyme is like a lock and that the substrate is like a key that fits into it due to its complementary shape

the enzyme active site is a fixed shape and due to random collisions, the substrate can collide and attach to the enzyme

this forms an enzyme substrate complex.

once the enzyme-substrate complex has formed, the charged
groups within the active site are thought to distort the substrate
and therefore lower the activation energy

the products are then released, and the enzyme active site is empty
and ready to be reused

103
Q

what is the induced fit model and what does it suggest?

A

this model suggests that the enzyme is like a glove and the substrate is like your hand; the empty glove is not exactly complementary in shape to your hand, but when your hand enters, it enables the glove to mold around your hand to become completely complementary

the enzyme active site is induced or slightly changes shape, to mould around the substrate

the formation of the enzyme substrate complex involves the enzyme moulding around the substrate, which puts a strain on the bonds and therefore lowers the activation energy

The products are then removed, and the enzyme active site returns to its original shape

104
Q

what is the accepted model for how enzymes work?

A

the induced fit model is the accepted model for how enzymes function

105
Q

what factors affect the rate of enzyme-controlled reactions?

A
  • temperature
  • pH
  • substrate concentration
  • enzyme concentration
  • inhibitors
106
Q

how does temperature the control rate of reaction?

A

if the temperature is too low, there is not enough kinetic energy for successful collisions between the enzyme and substrate

if the temperature is too high, enzymes denature, the active site changes shape and enzyme substrate complexes cannot form

107
Q

how does pH control rate of reaction?

A

too high or too low a pH will interfere with the charges in the amino acids in the active site.

this can break the ionic and hydrogen bonds holding the tertiary structure in place and therefore the active site changes shape.

therefore the enzyme denatures and fewer
enzyme-substrate complexes form.

108
Q

what happens to the active site when the enzymes are insufficient?

A

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

109
Q

what shape are competitive inhibitors?

A

the same shape as the substrate and can bind to the active site

110
Q

what do competitive inhibitors do?

A

prevents the substrate from binding and the reaction occurring

if you add more substrate this will out-compete the inhibitor, knocking them out of the active site

111
Q

where do non - competitive inhibitors bind to?

A

bind to the enzyme away from the active site (the allosteric site)

112
Q

what do non - competitive inhibitors cause the active site to do?

A

causes the active site to permanently change shape, and therefore the substrate can no longer bind, regardless of how much substrate is added

113
Q

what happens to competitive inhibitors at a high enough substrate concentration?

A

competitive inhibitors are knocked out of the active site and the rate of reaction will therefore return to the same as with no
inhibitor

114
Q

what is the rate of reaction with a non competitive inhibitor like?

A

will be lower at all substrate concentrations

115
Q

what structure of the proteins is an enzyme?

A

tertiary structure proteins

116
Q

what are the two types of lipids?

A

triglycerides and phospholipids

117
Q

how are triglycerides formed?

A

via condensation reactions

118
Q

what are triglycerides made up of?

A

one molecule of glycerol and three molecules of fatty acid

119
Q

what bonds are formed in triglycerides?

A

ester bonds are formed

120
Q

what does it mean by a saturated fatty acid?

A

the hydrocarbon chain has only single bonds between carbons

121
Q

what does it mean by an un-saturated fatty acid?

A

the hydrocarbon chain consists of at least one double bond between carbons

122
Q

what does an R-group on a triglyceride consist of?

A

R-groups are fatty acids which can be saturated or unsaturated

123
Q

why is a lot of energy stored in the triglyceride molecule due to its structure?

A

due to the large ratio of energy-storing carbon-hydrogen bonds compared to the number of carbon atoms

124
Q

why can triglycerides release water if they are oxidised due to their function?

A

due to the high ratio of hydrogen to oxygen atoms they act as a metabolic water source

125
Q

why do triglycerides not affect water potentials and osmosis due to their structure?

A

they are large and hydrophobic, making them insoluble in water

126
Q

why can a lot of triglycerides be stored without increasing the mass
and preventing movement due to their structure?

A

lipids have a relatively low mass

127
Q

why do phospholipids contain?

A

made of a glycerol molecule

two fatty acid chains

a phosphate group (attached to the glycerol)

128
Q

how do the two fatty acids also bond to the glycerol in a phospholipid?

A

via two condensation reactions

129
Q

what bonds are in a phospholipid?

A

two ester bonds.

130
Q

why does the hydrophilic ‘head’ of a phospholipid attract water?

A

it is charged

due to the phosphate being charged (polar), it repels other
fats

131
Q

is the fatty acid chain on a phospholipid non-polar or polar?

A

non-polar

it is known as the hydrophobic ‘tail’ and it repels water but will mix with fats

132
Q

why are phospholipids polar?

A

phospholipids have two charged regions

133
Q

what does a phospholipid bilayer make up?

A

the plasma membrane around cells

134
Q

how is the structure of a phospholipid bilayer positioned?

A

they are positioned so that the heads are exposed to water and
the tails are not

Biology (7 decks)

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