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Biological Molecules Flashcards

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1
Q

What is a monomer

A

Small repeating unit from which polymers are made

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2
Q

What is a polymer

A

Long chain of monomers joined together

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3
Q

Examples of monomers

A

Monosaccharides, amino acids, nucleotides

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4
Q

Describe the chemical reactions involved in the conversion of polymers to
monomers and monomers to polymers.
Give two named examples of polymers and their associated monomers to
illustrate your answer.

A

A condensation reaction joins monomers together and forms a
(chemical) bond and releases water;
2. A hydrolysis reaction breaks a (chemical) bond between
monomers and uses water;
dna is a polymer made of nucleotide monomers with phosphodiester bonds
proteins are polymers of amino acids with peptide bonds

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5
Q

What elements do all carbohydrates have and what are carbohydrates

A

C
H
O
Polymer

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6
Q

What are carbohydrates monomers and 3 examples

A

Monosaccharides
Glucose, fructose and galactose

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7
Q

What kind of sugar is glucose

A

Hexose sugar
Monosaccharides with 6 carbons

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8
Q

What are 2 isomers of glucose

A

Beta and Alpha

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9
Q

Isomers definition

A

Molecules with the same molecular formula as eachother but with atoms connected in a different

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10
Q

Where is OH and H on beta and alpha

A

OH ABBA - alpha below beta above
On alpha glucose : OH below on Carbon 1
On beta glucose: OH above on carbon 1

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11
Q

What does the OH group look like on left of alpha and beta glucose on carbon 4

A

HO

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12
Q

What reaction joins monomers/ monosaccharides together

A

Condensation reaction

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13
Q

Describe condensation reaction

A

2 mol join together forming chemical bond with an exclusion of water molecule

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14
Q

Condensation bet 2 monosaccharides

A

OH and H bond to form water molecule
This forms glycosidic bond

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15
Q

What is a disaccharide

A

Formed when 2 monosaccharides join

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16
Q

Name 3 disacharides and their monomers

A

Glucose + glucose —-> maltose
Glucose + fructose —-> sucrose
Glucose + galactose —-> lactose

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17
Q

What is a hydrolysis reaction

A

Splitting of polymer into monomers using water that breaks chemical bond

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18
Q

What can sugars be classified as

A

Reducing or non reducing

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19
Q

What are reducing sugars and name 5

A

Include all monosaccharides and maltose
Donate electrons
Glucose
Galactose
Maltose
Fructose
Ribose

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20
Q

Test for reducing sugars

A

Place 2cm^3 food sample in test tube
Add equal volume of Benedict’s reagent
Heat with boiling water in water bath

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21
Q

Positive test result

A

Forms coloured precipitate
Higher the conc of red sugar the deeper the colour
Blue —> green —> yellow —> orange —> brick red

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22
Q

More accurate way of doing red sug test

A

Filter solution and way precipitate
Use colourimeter

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23
Q

When would you do non red sugar test

A

If red sugars test is negative
Non red sugar may be present

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24
Q

Non red sug test

A

Get a new sample of test sol
Add dilute HCL
Heat in water bath until brought to boil
Neutralise with sodium hydrogen carbonate
Carry out Benedict’s test as you would for reducing sugar

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25
Q

Non red sugar postive test
+ negative test

A

Postive: Will form coloured precipitate
Negative : sol wil stay blue —> doesn’t contain any sug red or non red

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26
Q

What is a polysaccharide

A

Formed when 2 or more monosaccharides are joined by condensation reaction forming glycosidic bond

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27
Q

What is starch and where is it found

A

Main energy store in plants
Cells get energy from Glucose - excess glucose stored as starch in starch grains

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28
Q

What polysaccharides are in starch

A

Amylose and amylopectin

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29
Q

Amylose struc and function

A

Long unbranched chain of alpha glucose
Angles of glycosidic bond give coiled Struc - HELICAL
Makes it compact so it’s
Good for storage cus a lot can fit in small space

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30
Q

What bond is in amylose

A

1-4 glycosidic bond

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31
Q

Amylopectin Struc and function

A

Long branched chain of alpha glucose
Has side branches - enzymes can break mol easily to break glycosidic bond - glucose can be released quickly
Larger surface area for enzymes to attach too

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32
Q

Amylopectin bond

A

1-6 glycosidic bond + 1-4 glycosidic bond

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33
Q

Struc of starch rel to function

A

Insoluble - doesn’t affect cells water potential - water won’t enter via osmosis causing cell to swell
Large mol - can’t leave cell via diffusion
Helical - compact - can store lots of energy

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34
Q

Test for starch

A

Add iodine solution/ potassium iodide to test sample
If starch is present colour change from orange to blue black

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35
Q

Glycogen struc and function

A

Animals get energy from glycogen (stir of excess glucose)
Alpha glucose
Highly branched + lots of free ends
Hydrolysed quickly to prod lots of glucose (energy) in animals for movement
Compact mol - good for storage
1-4 +1-6 glycosidic bonds
Glycogen was more 1-6 glycosidic bonds than starch (more branched structure) insoluble-want affect cells water potential

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36
Q

Cellulose struc and function

A

Long unbranched chains of beta glucose that run parallel
Chains liked by hydrogen bonds that go on to form fibres - microfibrils
Structural support

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37
Q

Strength of h bonf

A

1 h Bond is weak but many hydrogen bonds are strong

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38
Q

2 types of lipid

A

Triglyceride
Phospholipid

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39
Q

Triglyceride struc

A

1 glycerol attached to 3 fatty acids

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40
Q

Fatty acid struc and components

A

Made of hydro carbons
Hydrophobic tails that repel water
Making lipids insol in water
Have
O = C — R
|
HO
HO at angle to C

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41
Q

How are triglycerides formed

A

Condensation of 1 glycerol to a fatty acid produced ester bond
Happend 2x more for 2 more fatty acids and 2 more ester bonds
Total 3 molecules of water produced
H2O prod from H in glycerol and HO in fatty acid

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42
Q

Fatty acids can either be …..

A

Saturated or unsaturated

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43
Q

Difference between fatty acids

A

Difference in hydrocarbon tails (R GROUP)

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44
Q

Saturated fatty acid

A

No double carbon bond

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45
Q

Unsaturated … + causes whag in chain

A

Have at least one double carbon to carbide bond , causing chain to kink

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46
Q

Phospholipid struc

A

1 phosphate group 1 glycerol 2 fatty acids
Phosphate group is hydrophilic
Fatty acid tail is hydrophobic

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47
Q

Uses of lipids

A

Waterproofing
Insulation
Protection
Energy
Phospholipid only - component of cell mem

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48
Q

Struc of triglyceride rel to function

A

1) Mainly energy storage molecules
Long hydrocarbon tails of fatty acids - lots of chem energy
Lipids contain ab 2x as much energy per gram as carbs

2) insol in water so doesn’t affect cells water pot . Water won’t enter via osmosis causing cell to swell
Triglycerides clump as insoluble droplets bc fatty acids hydrophobic tails face inward shielding themselves from water w glycerol heads

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49
Q

Phospholipid struc rel to function

A

Bilayer of cell mem
Heads hydrophilic ans tails hydrophobic so form double layer with heads facing outwards toward water on other side
Centre of bilayer is hydrophobic, water sol sub can’t easily pass so mem Acts as barrier to those sub

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50
Q

Test for lipids

A

Add sample to test tube
Add ethanol and shake
Add water
Milky white emulsion

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51
Q

Protien def

A

Long chain of amino acids

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52
Q

What’s formed whne 2 amino acids Join

A

Dipeptide

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53
Q

Whag is a poly pep

A

Formed whne 2 or more amino acids join together

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54
Q

What are protiens made up of

A

One or more poly pep

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55
Q

Struc of amino acids

A

R
|
H2N —C — COOH
|
H

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56
Q

R group

A

Variable group
Diff bet amino acids is their R group

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57
Q

How many amino acids do living things share

A

20

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58
Q

Condemnation of 2 amino acids

A

OH from COOH reacts w H on amine group of next amino acid forming water mol and leaving a peptide bond bet C and N

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59
Q

Primary structure

A

Specific seq of amino acids in polypeptide chain

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60
Q

Secondary struc

A

Folding due to H bonds making protien coil into alpha helix or beta pleated sheet

61
Q

Tertiary struc (final pro struc)

A

Further folding due to either ionic, hydrogen, disulfide bonds on diff parts of poly pep chains

62
Q

Quarternary struc

A

Several poly pep chains held together

63
Q

4 functions of pro

A

1) enzymes
2) antibodies - 2 light and 2 heavy polypeptide chains
3) transport protiens
4) structural pro - strong and contain crosslinks - keratin and collagen

64
Q

globular pro

A

enzymes (such as amylase), hormones (such as insulin) or proteins like haemoglobin. Globular proteins unravel and denature when the temperature or pH deviates from optimum levels. Globular proteins with prosthetic groups attached (such as haemoglobin) are referred to as conjugated proteins.

65
Q

fibrous pro

A

long and thin
Examples of fibrous proteins include collagen, keratin

66
Q
A
67
Q

Test for pro

A

Add sample to test tube
Add biuret sol
Colour change from blue to purple/lilac

68
Q

What are enzymes

A

Biological catalysts that speed up chemical reactions by lowering the activation energy without getting used up
Enzymes are protiens
Enzymes have a highly specific active site which binds to only one type of substance

69
Q

Why are enzymes highly specific

A

Due to tertiary struc giving unique 3D struc

70
Q

What happens if enzyme is catalysing a breakdown reaction

A

Fitting into the active site puts a strain on the bonds in sub so sub breaks up easily

71
Q

lock and key

A

Sub fits into enzyme like key fits into lock

72
Q

What’s wrong w lock and key

A

Enzyme and sub do fit together but it doesn’t talk about how e-s complex changes shape so locks fits even more tightly

73
Q

Induced fit model

A

BEFORE reaction active site not complementary to sub
Active site slightly alters its shape as substrate approaches
As enzyme changes shape it puts pressure on sub molecule distortingthe bonds in substrate
This causes the activation energy needed to break bonds to be lowered
Substrate fits more tightly
E-s complex formed
Sub broken down into products

74
Q

How can enzymes be affected by mutations

A

Random 🔼 in amino acid seq
Primary struc altered , position of bonding now diff …. 🔼 shape of active site so sub no longer binds
No reaction

75
Q

4 factors affecting enzyme activity

A

Temp
Ph
Enzyme conc
Sun conc

76
Q

Temp

A

Increase in temp causes particles to vibrate more due to gain in eK
Mol move faster = ⬆️ e-s complexes

If temperature increases too much = h bonds start to break shape of active 🔼
At first sub fits less easily
Then doesn’t fit at all
Enzymes denatured

77
Q

Ph + what is arrangement of active site det by

A

Ph = measure of H+ ion conc
🔼 in ph (H+ conc) Alter charges on amino acids at active site
Arrangement of active site partly det by hydrogen bond between amine and COOH groups
Bonds break leading to distortion in shape of active site so sub can no longer attach no longer complementary

78
Q

Denaturtion due to ph

A

If bonds in tertiary struc break enzyme will denature

79
Q

Enzyme conc

A

⬆️enzyme conc = ⬆️rate
More e-s complexes formed
But if sub conc limited
Not enough sub to bind to all the enzymes
Do ⬆️ enzyme conc has no effect

80
Q

Sub conc

A

⬆️sub conc = ⬆️ rate mostly
More collisions = more e-s complexes
True up until saturation point
Whereby all active sites used up
So ⬆️ sub conc has no effect
No active sites to bind to

81
Q

Competitive inhibition

A

A competitive inhibitor has a sim shape and struc to the sub mol
So are this complementary to enzymes active site and thus bind instead of of Sub
So n e-s complexes formed
⬆️ sub conc can ⬆️ rate as there’s a higher chance of sub binfing not inhibitor

82
Q

Non competitive inhibition

A

Binds to allosteric site of enzyme
This causes active site to change shape so sub mol are no longer complementary and cannot bind
⬆️ sub conc won’t have an effect on rate bc sub won’t be able to bind

83
Q

2 ways for Enzyme req prac

A

Measure how fast product of reaction is made
You can measure how fast the substrate is broken down

84
Q

How fast product is made

A

Catalyse catalyses the breakdown of hydrogen peroxide in to water and oxygen
So we work out vol of o2

85
Q

How do we measure vol of o2

A

Boiling tube w hydrogen peroxide sol and catalyse enzyme w bung w delivery tube attached into upside down measuring cylinder in trough of water

86
Q

How to set out expirment step 1
To measure how fast product is made

A

Set up boiling tube containing same vol and conc of hydrogen peroxide
Keep ph constant - add buffer sol

87
Q

Set up apparatus

A

Eg boiling tube w bung attached to delivery tube in upside down measuring cylinder in trough of water

88
Q

Step 3

A

But boiling tube in water bath set to diff temp
10, 20 , 30, up to 40 along with another tube containing catalyse

89
Q

Why do you wait 5 mins after step 3

A

So enzymes gets to right temp

90
Q

Step 4)

A

Use pipette to add Same vol and conc of catalyse to boiling tube then quickly attach bind and delivery tube

91
Q

Step 5

A

Record how much o2 prod in 1 min
Use stopwatch to measure time

92
Q

Step 6

A

Rep experiment ar each temp 3x
And use results to find an average vol of o2 prod
Calc av rate of reaction at each temp by diving vol of o2 prod by time taken

93
Q

Units for rate

A

Cm^3 s^-1

94
Q

What does enzyme amylayse catalyse break down of

A

Starch to maltose

95
Q

Apparatus of measuring how fast product broken down

A

A test tube - starch solution and amylayse enzyme
Dropping pippete
Spotting tile w drop of iodine in potassium iodide in it

96
Q

Step 1

A

Use pippete to drop mix of sol in one well at regular intervals until colour observed

97
Q

What colour does iodine sol turn

A

In presence of starch - blue black
No starch - orange brown

98
Q

How do we see how fast amylayse is working

A

Use stop watch to rec how long it takes for iodine sol to not turn blue black when mix added

99
Q

Step 2

A

Repeat experiment with different conc of amylayse
Repeat 3x for each conc

100
Q

What are dna and rna

A

Nucleic acids found in all living cells

101
Q

DNA

A

Stores genetic info

102
Q

RNA

A

Transfer genetic info from dna to ribosomes
Ribosomes make poly peptides (protiens) during translation

103
Q

Monomer for dna and rna

A

Nucleotide monomers that make up dna and rna polymers

104
Q

Nucleotide struc

A

A Pentose sugar w 5 carbons
Phosphate group
Nitrogenous base

105
Q

What is struc of nucleotide in dna

A

Deoxyribose sug
Phosphate group
Nitrogenous base (adenine thymine guanine and cytosine)

106
Q

Struc of rna nucleotide

A

Ribose sugar
Phosphate group
Nitrogenous base - Adenine uracil guanine and cytosine

107
Q

Nucleotides join to form what via what reaction

A

Via condensation reaction between phosphate group of one nucleotide and sugar of the next
Forming polynucleotide

108
Q

What bond forms and what does it consist of

A

Phosphodiester bond
Consisting of the phosphate group and 2 ester bonds

109
Q

Chain of sugars and phosphates known as ..

A

Sugar phosphate backbone

110
Q

DNA structure

A

2 antiparralel polynucleotide strands twist and join together to form double helix due to hydrogen bonding between complementary base pairs

Adenine has 2 h bonds wiht thymine
Cytosine has 3 h bonds wiht guanine

111
Q

describe dna structure (5)

A

Polymer of nucleotides
Each nucleotide formed from deoxyribose, a phosphate (group) and
an organic/nitrogenous base;
3. Phosphodiester bonds (between nucleotides);
4. Double helix/2 strands held by hydrogen bonds;
5. (Hydrogen bonds/pairing) between adenine, thymine and guanine and cytosine

112
Q

Describe how a phosphodiester bond is formed between two nucleotides
within a DNA molecule. (2)

A

Condensation (reaction)/loss of water;
2. (Between) phosphate and deoxyribose;
3. (Catalysed by) DNA polymerase;

113
Q

differences in structure of rna and dna

A

RNA is usually single-stranded, while DNA is double-stranded.
RNA is composed of ribonucleotides, which contain a ribose sugar, while DNA is composed of deoxyribonucleotides, which contain a deoxyribose sugar.
RNA contains the nitrogenous base uracil instead of thymine, which is found in DNA.
rna is shorter mol than dna

114
Q

who theorised semi conservative dna replication and chemical structure of dna

A

watson and crick

115
Q

what is semi conservative replication

A

half of the strands in each new molecule is from the original dna mol so there is genetic continuity bet generations of cells

116
Q

describe how dna is replicated

A

via semi conservative replication dna helicase enzyme is breaks hydrogen bonds and strands sep
helix unwinds and strands act as templates
free activated nucleotides attach to complementary base pairs
dna polymerase joins nuc on new strands via condesnation reaction
hydrogen bonds reform
2 new dna mol each with one og dna strand

117
Q

why new nucleotides can only be added in a 5’ to 3’
direction.

A

DNA polymerase;
2. (Which is) specific;
3. Only complementary with / binds to 3’ end (of strand);
Reject hydrogen bonds / base pairing
4. Shapes of 5’ end and 3’ end are different /
so anti parallel strands

118
Q

role of dna helicase

A

Breaks hydrogen bonds between base pairs/ AT and
GC/complementary bases

119
Q

Describe the role of DNA polymerase

A

) 1. Joins (adjacent DNA) nucleotides;
2. (Catalyses) condensation (reactions);
3. (Catalyses formation of) phosphodiester bonds (between adjacent
nucleotides);

120
Q

features of DNA and explain how each one is important in the
semi-conservative replication of DNA.

A

Weak / easily broken hydrogen bonds between bases allow two
strands to separate / unzip;
Two strands, so both can act as templates;
Complementary base pairing allows accurate replication;

121
Q

Contrast the structures of ATP and a nucleotide found in DNA

A

ATP has ribose and DNA nucleotide has
deoxyribose;
2. ATP has 3 phosphate (groups) and DNA
nucleotide has 1 phosphate (group);
3. ATP – base always adenine and in DNA
nucleotide base can be different

122
Q

what did evidence for semi conservative replication use

A

2 isotopes of nitrogen
light N-14
heavy N-15

123
Q

step 1

A

2 samples grown in nutrient broth containing isotopes

124
Q

step 2

A

sample of each dna taken and spun in centrifuge

125
Q

where does each isotope settle

A

14 - top
15 - bottom

126
Q

step 3

A

heavy nitrogen taken out and grown in light nitrogen left for one round of replication and then spun

127
Q

where did dna settle

A

in middle

128
Q

how did this prove semi conservative replication

A

new dna mol has one strand of old dna w heavy and one strand w light

129
Q

what would it look like if rep was conservative

A

heavy dna at bottom
light dna on top

130
Q

water mol struc

A

one atom of oxygen w delta negative 2 atoms of hydrogen w delta positive
so water polar
o atoms attract h atoms attraction called hydrogen bonding

131
Q

Explain five properties that make water important for organisms.

A

A metabolite in condensation/hydrolysis/ photosynthesis/respiration;
2. A solvent so (metabolic) reactions can occur
OR
A solvent so allowing transport of substances;
3. High (specific) heat capacity so buffers changes in temperature;
4. Large latent heat of vaporisation so provides a cooling effect (through
evaporation);
5. Cohesion (between water molecules) so supports columns of water in plants (transpiration streams)
6. Cohesion (between water molecules) so produces surface tension supporting small organisms

132
Q

State and explain the property of water that can help to buffer changes in
temperature

A

(water has a relatively) high (specific) heat capacit
Can gain / lose a lot of heat / energy without changing temperature;

133
Q

Give two properties of water that are important in the cytoplasm of cells.
For each property of water, explain its importance in the cytoplasm.

A

Polar molecule; Acts as a (universal) solvent;
Reactive;
Takes place in hydrolysis / condensation / named reaction;

134
Q

what is atp

A

immediate source of energy

135
Q

when its made where does it go

A

diffuses to parts of cell that needs energy

136
Q

where is energy in atp stored

A

bonds bet phosphate groups rel via hydrolysis

137
Q

Describe how an ATP molecule is formed from its component molecules.

A

condensation between 3 phosphate groups, adenine base and ribose sugar
catalysed by atp synthase

138
Q

how and when is atp broken down

A

when energy is needed by cell atp hydrolayse enzyme breaks phosphate bond

139
Q

products of atp hydrolysis

A

ADP + Pi

140
Q

ways in
which ATP is a suitable energy source for cells to use.

A

little energy lost as heat as hydrolysis coupled with other energy req reactions so energy used to make that reaction happen
Phosphorylates other compounds, making them more reactive;
rapidly re synthesised

141
Q

how is atp resynthesised

A

From ADP and phosphate;
By ATP synthase;
3. During respiration/photosynthesis;

142
Q

what is an inorganic ion

A

doesnt contain carbon
are a few exeptions

143
Q

name 4 inorganic ions

A

iron ions
hydrogen ions
sodium ions
phosphate ions PO4^3-

144
Q

FE2+

A

haemoglobin made of 4 polypep chains w fe2+ ion in centre
Haemoglobin binds/associates with oxygen in rbc

145
Q

H+

A

ph calc based on conc of ion
more ions = lower ph + more acidic

146
Q

na+

A

Co-transport of glucose/amino acids (into cells);
3. (Because) sodium moved out by active transport/Na – K pump;
4. Creates a sodium concentration/diffusion gradient;
5. Affects osmosis/water potential;

147
Q

po43-

A

Joins nucleotides/in phosphodiester bond/in backbone of
DNA/RNA/in nucleotides;
8. Used in/to produce ATP;
Reject ‘energy produced’
9. Phosphorylates other compounds (usually) making them more
reactive;

148
Q

how does struc of protein dep on amino acids it contains

A
  1. Structure is deternmined by (relative) position of
    amino acid/R group/interactions;
  2. Primary structure is sequence/order of amino
    acids;
  3. Secondary structure formed by hydrogen
    bonding (between amino acids);
  4. Tertiary structure formed by interactions
    (between R groups);
  5. Creates active site in enzymes
    OR
    Creates complementary/specific shapes in
    antibodies/carrier proteins/receptor (molecules);
  6. Quaternary structure contains >1 polypeptide
    chain
    OR
    Quaternary structure formed by
    interactions/bonds between polypeptides;
149
Q

describe the roles of iron ions, sodium ions and phosphate ions in cells

A

Iron ions
1. Haemoglobin binds/associates with
oxygen
OR
Haemoglobin transports/loads
oxygen;
Sodium ions
2. Co-transport of glucose/amino
acids (into cells);
3. (Because) sodium moved out by
active transport/Na – K pump;
4. Creates a sodium
concentration/diffusion gradient;
5. Affects osmosis/water potential;
Phosphate ions
6. Affects osmosis/water potential;
7. Joins nucleotides/in
phosphodiester bond/in backbone
of DNA/RNA/in nucleotides;
8. Used in/to produce ATP;
9. Phosphorylates other compounds
(usually) making them more
reactive;
10. Hydrophilic/water soluble part of
phospholipid bilayer/membrane;

Bio Aqa (9 decks)

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