Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

A LEVEL BIO > topic 1 - biological molecules > Flashcards

topic 1 - biological molecules Flashcards

You may prefer our related Brainscape-certified flashcards:
Biology 101 flashcards
1
Q

monomers

A

smaller units from which larger molecules are made

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

polymers

A

molecules made from a large number of monomers joined together in a chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

how many bonds can each carbon atom form?

A

4 covalent bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

the molecules of life all contain….

A

carbon, hydrogen and oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

what are the four main groups of carbon-based molecules common to all life forms?

A

carbohydrates, lipids, proteins, nuclei acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

carbohydrates: uses

A

-respiratory substrates
-energy for cells
-structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

lipids: uses

A

-respiratory substrates
-form bilayer
-sometimes make up hormones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

proteins: uses

A

-main component of many cellular structures
-form enzymes and chemical messengers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

nucleic acids: uses

A

-form polymers (DNA and RNA) which make up the genetic material of organisms
-code for the sequence of amino acids which make up all proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

how many amino acids build up protein

A

20

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

condensation reaction

A

joins two monomers together with a covalent bond and produces a water molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

hydrolysis

A

breaks the covalent bond between two monomers and involves the use of a water molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what elements are common to all the molecules of life?

A

carbon, hydrogen, nitrogen, oxygen, phosphorus & sulfur

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

which molecule forms part of the plasma membrane?

A

phospholipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what are monosaccharides?

A

individual sugar molecules (monomers) that make up disaccharides and polysaccharides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

hexose sugar

A

A sugar made up of 6 carbons.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

pentose sugar

A

a sugar made up of 5 carbons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

how many isomers can glucose form?

A

two:
a-glucose
b-glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

difference between structure of alpha and beta glucose:

A

alpha:
h over oh

beta:
oh over h

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

how are disaccharides formed?

A

formed when two monosaccharides join through a condensation reaction forming a glycosidic bond between the two OH groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

glucose + glucose

A

maltose (reducing)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

glucose + galactose

A

lactose (reducing)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

glucose + fructose

A

sucrose (non reducing)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

when is a polysaccharide formed?

A

when more than two monosaccharides are joined together by condensation reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

what is starch made from?

A

the monosaccharide alpha glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

structure of starch:

A

mixture of two polysaccharides: amylose and amylopectin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

structure of amylose

A

-long unbranched forms
-coiled
-1-4 glycosidic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

structure of amylopectin

A

long branched chain due to 1-6 glycosidic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

properties of amylose

A

coiling makes it compact and stores more in a smaller space

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

properties of amylopectin

A

branches increase surface area for enzymes to hydrolyse glycosidic bonds allowing glucose to be released quickly

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

uses of starch:

A

-plants → starch to store excess glucose
too large to leave cells and insoluble (doesn’t dissolve in water - this also means it does not affect water potential)

-starch can be hydrolysed to release glucose for respiration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

monosaccharide of glycogen

A

alpha glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

structure of glycogen

A

-a long, branched chain with lots of side branches (more than amylopectin)
-1-6 glycosidic bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

properties of glycogen

A

-lots of branches increase surface area for enzymes to hydrolyse glycosidic bonds allowing glucose to be released quickly
-compact molecule, good for storage

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

uses of glycogen

A

-animals store excess glucose as glycogen in muscles and in the liver.
-glycogen is an energy store as it can be hydrolysed to release glucose quickly when needed for respiration e.g during exercise

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

monosaccharide of cellulose

A

beta glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

structure of cellulose

A

-long unbranched straight chains
-1-4 glycosidic bonds
-cellulose chains are linked together by hydrogen bonds between the glucose molecules in each chain to form thicker fires called microfibrils

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

properties of cellulose

A

-hydrogen bonds between the cellulose chains make the microfibrils very strong but still flexible allowing them to provide support

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

uses of cellulose

A

-major structural component in the cell walls of plants
-provides support and allows cells to become turgid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

one way starch molecules are adapted for their function in plant cells

A

insoluble so that they don’t affect water potential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

what is the group of carbohydrates?

A

hydroxyl

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

one advantage of storing starch rather than glucose in potato cells

A

plants use starch to store excess glucose, it’s insoluble, so potato cells save space and don’t affect water potential

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

most common disaccharides

A

maltose
lactose
fructose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

where is maltose found?

A

in germinating seeds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

where is lactose found?

A

in mammalian milk

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

where is fructose found?

A

used to transport sugar around plants

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

are lipids polymers?

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

which two types of lipids do we look at?

A

-triglycerides
-phospholipids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

components of triglycerides

A

a glycerol molecule and three fatty acid chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

bonds of triglycerides

A

ester bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

properties of triglycerides

A

-the fatty acid chains are hydrophobic (repel water) which makes lipids insoluble in water
-they bundle together as insoluble droplets because the tails face inwards, and the glycerol heads shield them from the water
-the hydrocarbon fatty acid chains can be saturated or unsaturated

(triglycerides are entirely hydrophobic)
-non-polar, hydrophobic molecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

components of phospholipids

A

a glycerol molecule, a phosphate group and two fatty acid chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

bonds of phospholipids

A

ester bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

properties of phospholipids

A

-the phosphate group is hydrophilic (attracts water)
- he fatty acid chains are hydrophobic (repel water).
-this allows phospholipid to form bilayers which make up membranes in and around cells

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

saturated fatty acids

A

-don’t have any double bonds between their carbon atoms
-the fatty acid has all the hydrogens it can hold

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

unsaturated fatty acids

A

-have double bonds between carbon atoms which means they contain fewer hydrogen atoms
-the double bond also causes the chain to bend
-unsaturated fatty acid chains can contain one (mono) or many (poly) carbon double bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

phospholipid bilayer

A

-phospholipid heads are hydrophilic and their tails are hydrophobic so when placed in water they form a double layer with the heads facing outwards towards the water and their tails facing inwards away from the water
-the centre of the bilayer is therefore hydrophobic so water soluble substances cannot easily pass through
-this creates a barrier and allows separation of solutions and can create different conditions either side of the membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

four roles of lipids

A

-hormones
-insulation
-energy reserve
-cushion vital organs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

what are proteins?

A

polymers made up of monomers known as amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

components of amino acids:

A

amino group (H^2n)
carboxylic group (COOH)
variable group (R)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

what is the only difference between each amino acid?

A

the variable R group/side chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

what happens when two amino acids join in a condensation reaction?

A

-a dipeptide forms
-a water molecule is released
-the peptide bond forms between the amine group of one amino acid and the carboxyl group of the other

63
Q

what is more than two amino acids joined together?

A

polypeptide

64
Q

how can dipeptides and polypeptides be broken down?

A

hydrolysis

65
Q

how many levels can single chain polypeptides have?

A

three (primary, secondary and tertiary)

66
Q

primary structure (chain of amino acids)

A

-the number and sequence of amino acids in the polypeptide chain can determine the 3D shape or tertiary structure and can affect the shape of the active site in enzymes

67
Q

secondary structure (pleated sheet)

A

-hydrogen bonds form between amino acids in the chain, this causes it to coil into an a-helix or fold into a -pleated sheet
-the many hydrogen bonds make these structures stable

68
Q

tertiary structure

A

the 3D shape of the polypeptide chain:

-creates a specific shape due to the sequence of amino acids in the chain -hydrogen bonds, ionic bonds and disulphide bridges (covalent bonds) form between R groups
-a change to the sequence of amino acids would affect the tertiary structure as these bonds would form in different places
-all enzymes, antibodies and some hormones have tertiary structure

69
Q

quartenary structure (+ example)

A

-if proteins are made of more
than one polypeptide chain, then they are joined together to create quaternary structure
-antibodies and haemoglobin are examples of these

70
Q

what are enzymes?

A

biological catalysts
-increase rate of reaction by lowering the activation energy of the reaction they catalyse
-3D tertiary structured globular proteins whose shape is determined by the primary sequence of amino acids

71
Q

what are enzymes specific to?

A

the substrates that they bind to

72
Q

what happens when enzymes and substrates bind?

A

they form an enzyme substrate complex

73
Q

induced fit model

A

when an enzyme’s structure is altered so that the active site of the enzyme fits around the substrate that it has binded to

74
Q

how does temperature affect the rate of enzyme controlled reactions?

A

-rate of reaction increases up to the optimum temperature as the kinetic energy of the enzyme increases
-above the optimum temperature, rate of reaction decreases
-the enzyme becomes denatured

75
Q

how does pH affect the rate of enzyme controlled reactions?

A

-pH affects the enzymes shape as it can disrupt the bonds in the tertiary structure of the enzyme
-all enzymes work at different optimum pH’s, at pH’s that aren’t these, the enzymes don’t work at their best

76
Q

how does enzyme concentration affect the rate of enzyme controlled reactions?

A

-the rate of reaction increases as enzyme concentration increases as there are more active sites for substrates to bind to
-however increasing the enzyme concentration beyond a certain point has no effect on the rate of reaction as there are more active sites than substrates so substrate concentration becomes the limiting factor

77
Q

how does substrate concentration affect the rate of enzyme controlled reactions?

A

-as concentration of substrate increases, rate of reaction increases as more enzyme-substrate complexes are formed
-beyond a certain point the rate of reaction no longer increases as enzyme concentration becomes the limiting factor

78
Q

competitive inhibitors

A

-compete with the substrate for the active site
-the inhibitor molecule has a similar shape to the substrate molecule & competes with the substrate to bind to the active site of an enzyme
-they block the active site so the substrate cannot bind, and no ES complexes are formed

79
Q

non competitive inhibitors

A

-non competitive do not bind to the active site
-the inhibitor molecule can bind to a site on an enzyme that is not the active site (allosteric site)
-binding of the inhibitor to the alternative site results in a change in shape) of the active site
-the enzyme is no longer able to bind to its substrate

80
Q

how to reverse the effects of a competitive inhibitor

A

increasing the concentration of the substrate, the substrate will out-compete the inhibitor for the active sites

81
Q

can you reverse the effects of a non competitive inhibitor?

A

no, increasing the concentration of the substrate will not affect the rate of reaction because they cannot bind to the active site

82
Q

what does ATP consist of?

A

ribose, adenine and three phosphate groups

83
Q

when is energy released from ATP?

A

when ATP is hydrolysed to form ADP and a phosphate molecule

84
Q

what is the process of releasing energy from ATP hydrolysed with?

A

ATP hydrolase

85
Q

where does the energy in ATP come from?

A

the bonds between the phosphate molecules

86
Q

why is energy released quickly from
ATP?

A

-the bonds between phosphate molecules are very unstable and have a low activation energy
-the breaking of these is quick and releases a considerable amount of energy

87
Q

why is ATP more desirable than glucose?

A

-ATP is an immediate source of energy
-ATP can be broken down in a single step to release a manageable quantity of energy

88
Q

why isn’t ATP stored in large quantities?

A

it can easily be reformed from ADP in seconds

89
Q

how is ATP used?

A

-in metabolic processes
-for movement
-in active transport

90
Q

what is water a major component of?

A

all cells

91
Q

why is water a polar molecule?

A

-there is an uneven distribution of charge within the molecule
-the hydrogen atoms are more positive than the oxygen atom causing one end of the molecule to be more positive than the other

92
Q

what part does water play in metabolic reactions?

A

-it is a metabolite in metabolic reactions (eg: condensation and hydrolysis)

93
Q

water has a high…? what does this mean?

A

-it has a high heat specific capacity
-this is because water molecules stick together with hydrogen bonds meaning that a lot of energy is required to break these bonds
-this helps to minimise temperature fluctuations in living things therefore it acts as a buffer

94
Q

what does water having a relatively high latent heat of vaporisation mean?

A

hydrogen bonding means that it requires a lot of energy to evaporate 1 gram of water, meaning evaporation of water provides a cooling effect with little water loss

95
Q

is water a solvent, solute or solution?

A

solvent, it aids diffusion

96
Q

cohesion tension theory

A

1) hydrogen bonds between water molecules result in cohesion

2) water moves from the roots to the leaves because of a gradient

3) this gradient is present due to the constant loss of water from the leaves by transpiration and the constant uptake of water at the roots by osmosis

4) the evaporation of water into the air spaces in the leaves creates tension in the xylem tissue which is transmitted all the way down the plant because of the cohesive nature of water molecules

5) the cohesive force results in a continuous column of water with high tensile strength

6) the adhesive force stops the water column from pulling away from the walls of the xylem vessels

97
Q

what colour is benedict’s solution?

A

blue

98
Q

what does benedict’s reagent contain?

A

copper (II) sulfate ions

99
Q

what happens to copper (II) sulfate ions in the presence of a reducing sugar?

A

copper (I) oxide forms

100
Q

property of copper (I) oxide that relates to benedict’s test

A

copper (I) oxide is not soluble in water, so it forms a precipitate

101
Q

method of benedict’s test:

A

1) heat a sample in a test tube with benedict’s

2) if a reducing sugar is present, a coloured precipitate will form

102
Q

how much benedict’s should be used and why?

A

an excess of benedict’s solution is used so that there is more than enough copper (II) sulfate present to react with any sugar present

103
Q

colour range for benedict’s test:

A

a colour scale from blue (no reducing sugar), through green, yellow and orange (low to medium concentration of reducing sugar) to brick-red (a high concentration of reducing sugar)

104
Q

benedict’s test equipment

A

benedict’s
test tube
bunsen burner or water bath

105
Q

non reducing sugar example

A

sucrose

106
Q

test for non reducing sugars

A

-add dilute hydrochloric acid to the sample and boil in a water bath
-neutralise the solution with an alkali sodium hydrogencarbonate
-use a suitable indicator to see when the solution has been neutralised, and then add a little more sodium hydrogencarbonate
-carry out the benedict’s test as normal

107
Q

why is excess hydrogen carbonate added?

A

the conditions need to be slightly alkaline for the benedict’s test to work

108
Q

why is acid added?

A

will hydrolyse any glycosidic bonds present in any carbohydrate molecules

109
Q

test for starch

A

1) add a few drops of iodine to the sample

2) blue-black colour is produced

110
Q

what does DNA stand for?

A

deoxyribonucleic acid

111
Q

what does RNA stand for?

A

ribonucleic acid

112
Q

what are both dna and rna?

A

-nucleic acids
-needed to build proteins
-found in all living cells

113
Q

what is the function of dna?

A

-to store genetic information (the instructions an organism needs to grow and develop)

114
Q

what is the function of rna?

A

to transfer genetic information from the DNA to the ribosomes

115
Q

what is a nucleotide?

A

a type of biological molecule

116
Q

what is a nucleotide made up of?

A

-a pentose sugar
-a nitrogenous base
-a phosphate group

117
Q

why are nucleotides important?

A

they’re the monomers that make up DNA and RNA

118
Q

what makes up a DNA nucleotide?

A

-a deoxyribose sugar
-a phosphate group
-the base on each nucleotide can vary

119
Q

what are the four DNA bases?

A

A - adenine
T - thymine
C - cytosine
G - guanine

120
Q

what makes up a RNA nucleotide?

A

-ribose sugar
-a phosphate group
-one of four different bases

121
Q

what are the four RNA bases?

A

A - adenine
U - uracil (replaces thymine)
C - cytosine
G - guanine

122
Q

what is a polynucleotide?

A

-a polymer of nucleotides
-both DNA and RNA nucleotides form polynucleotides

123
Q

how do nucleotides join up?

A

via a condensation reaction between the phosphate group of one nucleotide and the sugar of another

124
Q

what bond is between nucleotides

A

a phosphodiester bond (consisting of the phosphate group and two ester bonds)

125
Q

what is the chain of sugars and phosphates is known as?

A

the sugar-phosphate backbone

126
Q

two DNA polynucleotide strands join together by…

A

hydrogen bonding between the bases

127
Q

what is complementary base pairing?

A

each base can only join with one particular partner

128
Q

what are the base pairs?

A

A-T
C-G

129
Q

how does the distribution of bases work?

A

% of C = % of G
% of A = % of T/U

130
Q

how many hydrogen bonds are between A-T?

A

2 hydrogen nonds

131
Q

how many hydrogen bonds are between C-G?

A

3 hydrogen bonds

132
Q

how is the double helix structure formed?

A

two antiparallel polynucleotide strands twist

133
Q

structure of RNA

A

-RNA is made from a single polynucleotide chain
-shorter than most DNA polynucleotides

134
Q

when and why does DNA copy itself?

A

DNA copies itself before cell division so that each new cell has the full amount of DNA.

135
Q

the concept of semi-conservative replication and what it means

A

-one strand in each new DNA molecule is from the original DNA molecule
-this means that there’s genetic continuity between generations of cells

136
Q

steps of semi conservative replication (transcription)

A

1) the enzyme DNA helicase breaks the hydrogen bonds between bases, the helix unwinds to form two single strands

2) each original single strand acts as a template for a new strand. free DNA bases are attracted to their complementary exposed bases on each original template strand

3) condensation reactions join the nucleotides of the new strands together catalysed by the enzyme DNA polymerase. hydrogen bonds form between the bases on the original and new strands

4) each new DNA molecule contains one strand from the original DNA molecule and one new strand

137
Q

which two structural forms do nucleotides occur in?

A

purines and pyrimidines

138
Q

what is a purine (+ examples)

A

double ring structure
(adenine and guanine)

139
Q

what are pyrimidines? (+ examples)

A

single ring structure
(cytosine, thymine, uracil)

140
Q

the ends of DNA

A

each DNA polynucleotide strand is said to have a 3’ end and a 5’ end (these numbers relate to which carbon on the pentose sugar could be bonded with another nucleotide)
-the strands are antiparallel: one is known as the 5’ to 3’ strand and the other is known as the 3’ to 5’ strand

141
Q

what did the simplicity of RNA mean?

A

many scientists doubted that it carried the genetic code

142
Q

what are the components of ribosomes?

A

RNA and proteins

143
Q

properties of the RNA in ribsomes

A

the rRNA in ribsomes catalyses the formation of peptide bonds between amino acids

144
Q

where is mRNA in the ribsome?

A

mRNA sits between the two subunits

145
Q

watson & crick

A

-two scientists who worked together to confirm the double-helix structure of DNA in 1953
-came up with the theory of semi-conservative DNA replication

146
Q

meselson and stahl’s experiment

A

1) two samples of bacteria were grown, one in a nutrient broth with light nitrogen, one in a broth with heavy nitrogen. as the bacteria reproduced, they took up nitrogen from the broth to help make nucleotides for new DNA, so the nitrogen gradually became part of the bacteria’s DNA

2) a sample of DNA was taken from each batch of bacteria, and spun in a centrifuge. the DNA from the heavy nitrogen bacteria settled lower down the centrifuge tube than the DNA from the light nitrogen bacteria

3) then the bacteria grown in the heavy nitrogen broth were taken out and put in a broth containing only light nitrogen. the bacteria were left for one round of DNA replication, and then another DNA sample was taken out and spun in the centrifuge

4) the DNA settled out in the middle, showing that the DNA molecules contained a mixture of heavy and light nitrogen. the bacterial DNA had replicated semi-conservatively in the light nitrogen

147
Q

what is the emulsion test for?

A

lipids

148
Q

emulsion test steps:

A

1) add ethanol and shake

2) next, pour the entire solution into a test tube containing water

3) check for formation of a milky white emulsion

149
Q

why does emulsion form?

A

-lipids are insoluble in water, so they will not mix with the water
-any lipids present in your sample will float to the top and form a milky white emulsion
-the greater the concentration of lipids in your sample, the more apparent the milky colour will become

150
Q

what is the biuret test for?

A

proteins

151
Q

first step of the biuret test:
(+ explanation)

A

make the solution alkaline
-to properly test for proteins, your test solution needs to be alkaline
-add a few drops of sodium hydroxide to your solution

152
Q

second step of the biuret test:
(+ explanation)

A

add copper (II) sulphate

153
Q

third step of the biuret test:
(+ explanation)

A

observe the colour change of your test solution

blue = no protein present in your sample
purple = protein is present

A LEVEL BIO (12 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions