biological molecules Flashcards

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1
Q

What is a molecule?

A

The complex formed when two or

more atoms bond together

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2
Q

What are covalent bonds?

A
Bond that occur when two atoms 
share a pair of electrons. The 
electrons used to form bonds are 
unpaired and present in the outer 
orbitals of the atoms
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3
Q

What are covalent bonds?

A
Bond that occur when two atoms 
share a pair of electrons. The 
electrons used to form bonds are 
unpaired and present in the outer 
orbitals of the atoms
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4
Q

What are the bonding rules for
carbon, nitrogen, oxygen and
hydrogen atoms?

A
  • Carbon atoms form 4 bonds
  • Nitrogen atoms form 3 bonds
  • Oxygen atoms form 2 bonds
  • Hydrogen atoms form 1 bonds
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5
Q

What is an ion?

A

An atom or molecule with an overall
electric charge because the total
number of electrons is not equal to
the total number of protons

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6
Q

What is an ionic bond?

A
A chemical bond that involves the 
donating of an electron from one 
atom to another, forming positive 
and negative ions held together by 
the attraction of the opposite 
charges
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7
Q

What is a cation?

A

An atom or molecule that loses one
or more electrons giving it a net
positive charge

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8
Q

What is an anion?

A

An atom or molecule that gains one
or more electrons giving it a net
negative charge

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9
Q

What are ions in solution

called?

A

Electrolytes

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10
Q

List all of the important cations

in living organisms

A
  • Calcium ions (Ca2+)
  • Sodium ions (Na+)
  • Potassium ions (K+)
  • Hydrogen ions (H+)
  • Ammonium ions (NH4+
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11
Q

List all of the important anions

in living organisms

A
  • Nitrate ions (NO3-)
  • Hydrogen carbonate ions (HCO3-)
  • Chloride ions (Cl-)
  • Phosphate ions (PO43-)
  • Hydroxide ions (OH-)
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12
Q
What are the following cations 
necessary for? 
1. Calcium ions 
2. Sodium ions 
3. Potassium ions 
4. Hydrogen ions 
5. Ammonium ions
A
1. Nerve impulse transmission and 
muscle contractions
2. Nerve impulse transmission and 
kidney function
3. Nerve impulse transmission and 
stomatal opening
4. Catalysis of reactions and pH 
determination
5. Production of nitrate ions by 
bacteria
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13
Q
What are the following anions 
necessary for? 
1. Nitrate ions 
2. Hydrogen carbonate ions 
3. Chloride ions 
4. Phosphate ions 
5. Hydroxide ions
A
1. Nitrogen supply to plants for 
amino acid and protein formation
2. Maintenance of blood pH
3. Balance positive charge of 
sodium and potassium ions in 
cells 
4. Cell membrane formation, 
nucleic acid and ATP formation, 
bone formation
5. Catalysis of reactions and pH 
determination
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14
Q

List the 4 biological molecules
and the element present in
each of them

A
• Carbohydrates - carbon, 
hydrogen, and oxygen usually in 
the ration Cx(H2O)x
• Lipids - carbon, hydrogen, and 
oxygen 
• Proteins - carbon, hydrogen, 
oxygen, nitrogen, and sulphur
• Nucleic acids - carbon, hydrogen, 
oxygen, nitrogen, and phosphorus
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15
Q

What are the monomers in
carbohydrates and proteins
called?

A

In carbohydrates the monomers
are sugars (saccharides) monosaccharides
• In proteins the monomers are
amino acids

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16
Q

What are the monomers in
carbohydrates and proteins
called?

A

In carbohydrates the monomers
are sugars (saccharides)
• In proteins the monomers are
amino acids

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17
Q

Why are some molecules

polar?

A
• In covalent bonds the electrons are 
not always shared equally by the 
atoms of different elements
• The atoms with the greater share 
of negative electrons will be 
slightly negative compared with 
the other atom in the bond, which 
will be slightly positive 
• Polar molecules have regions of 
negativity and regions of positivity
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18
Q

Why is water a polar

molecule?

A
• Oxygen always has a much 
greater share of electrons in an OH bond
• Many organic molecules contain 
hydroxyl (OH) groups, and so are 
slightly polar; water is an example
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19
Q

What are hydrogen bonds, and

what causes them?

A
Hydrogen bonds are relatively 
weak interactions
• They are caused by polar 
molecules interacting with each 
other and forming bonds - 
hydrogen bonds
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20
Q

List the properties of water

A
  • Liquid
  • Density
  • Solvent
  • Cohesion and surface tension
  • High specific heat capacity
  • High latent heat of vaporization
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21
Q

Why is water a liquid at room

temperature?

A

• The hydrogen bonds between
water molecules make it more
difficult for them to escape to
become a gas

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22
Q

What is the importance of
water being a liquid at room
temperature, to living
organisms?

A
• Provides habitats for living things 
in rivers, lakes and seas
• Forms a major component of the 
tissues in living organisms 
• Provides a reaction medium for 
chemical reactions
• Provides an effective transport 
medium e.g. in blood and vascular 
tissue
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23
Q

Describe how the density of
water changes, as H2O
changes state

A
Usually the solid is more dense than 
the liquid form of a substance.
However ice is less dense than 
water because as water goes from 
4C to freezing point, the water 
molecules form a structure that is 
less dense than liquid water
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24
Q

What is the importance of
water’s density to living
organisms?

A
If water was less dense, aquatic 
organisms would find it very 
difficult to float
Ice floats on water so:
• Aquatic organisms have a stable 
environment to live through in 
winter
• Ponds are insulated against 
extreme cold because the ice layer 
reduces heat loss from the pond
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25
Q

Why is water a good solvent?

A
• As it is polar, the positive and 
negative parts of the water 
molecules are attracted to the 
oppositely charged parts of the 
solute
• Water molecules cluster around 
the charged parts of the solute 
molecules or ions, which helps to 
separate them and keep them 
apar
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26
Q

What is the importance of
water being a good solvent to
living organisms?

A
• Molecules and ions can move 
around and react together in water 
e.g. as in the cytoplasm of cells, 
which is >70% water
• molecules and ions can be 
transported around living things 
whilst dissolved in water
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27
Q

Describe cohesion and surface

tension of water

A
• Water molecules demonstrate 
cohesion because hydrogen 
bonding between the molecules 
pulls them together 
• Water molecules demonstrate 
surface tension because they are 
more attracted to the water 
molecules beneath them than air 
molecules above, so the water 
contacts, giving the surface of the 
water the ability to resist a force 
applied to it
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28
Q

What is the importance of
cohesion and surface tension
of water to living organisms?

A
Columns of water in plant vascular 
tissue are pulled up the xylem 
tissue together from the roots due 
to cohesion 
• Insects like pond-skaters can walk 
on water due to surface tension
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29
Q

Why does water have a high

specific heat capacity?

A
• Water molecules are held together 
quite tightly by hydrogen bonds
• Therefore you need to put in a lot 
of heat energy to increase their 
kinetic energy and temperature 
• This means that water doesn’t 
heat up or cool down easily
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30
Q

What is the importance of the
high specific heat capacity of
water to living organisms?

A
• Living things need a stable 
temperature for enzyme-controlled 
reactions to happen properly
• Aquatic organisms need a stable 
environment in which to live
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31
Q

Why does water have a high

latent heat of vaporisation?

A
Because the water molecules are 
held together by hydrogen bonds, a 
relatively large amount of energy is 
needed for water molecules to 
evaporate
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32
Q

what is the importance of the
high latent heat of
vaporisation of water to living
organisms?

A
Water can help to cool living things 
and keep their temperature stable 
e.g.
• Mammals are cooled when sweat 
evaporates
• Plants are cooled when water 
evaporates from mesophyll cells
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33
Q

What is the importance of
water’s role as a reactant to
living organisms

A
It is a reactant in reactions such as 
photosynthesis, and in hydrolysis 
reactions such as digestion of 
starch, proteins and lipids
• Plays a very important role in the 
digestion and synthesis of large 
biological molecules
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34
Q

What are carbohydrates?

A
Organic polymers composed of the 
elements carbon, hydrogen and 
oxygen, usually in the ration 
Cx(H2O)y. Also known as 
saccharides or sugars
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35
Q

Define the following:

  1. Monosaccharide
  2. Disaccharide
  3. Polysaccharide
A
1. A single sugar molecule e.g. 
glucose, fructose and ribose
2. A molecule comprising two 
monosaccharides joined 
together by a glycosidic bond
3. A polymer made up of many 
monosaccharides e.g. glycogen, 
cellulose and starch
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36
Q

Describe glucose

A
• C6H12O6
• Hexose monosaccharide (because 
it has 6 carbons)
• Polar and soluble in water due to 
the hydrogen bonds that form 
between the OH group and water 
molecules 
• Means glucose is dissolved in the 
cytosol of the cell
2 variations 
• Alpha glucose - OH group is 
below carbon 1 
• Beta glucose - OH group is above 
carbon 1
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37
Q

How do alpha glucose
molecules react with each
other?

A
• The OH groups on C1 and C4 
reacted forming a 1,4 glycosidic 
bond (covalent)
• Condensation reaction because a 
water molecule is formed (lost)
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38
Q
What do the following 
combinations form? 
1. a-glucose + a-glucose 
2. a-glucose + fructose 
3. B-galactose + a-glucose 
4. B-glucose+ B-glucose
A
  1. Maltose
  2. Sucrose
  3. Lactose
  4. Cellobiose
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39
Q

What are pentose
monosaccharides? Give
examples

A
• Sugars that contain 5 carbon 
atoms 
• e.g. ribose which is the sugar 
present in RNA nucleotides
• e.g. deoxyribose which is the 
sugar present in DNA nucleotides
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40
Q

What is starch?

A

A polysaccharide formed from alpha
glucose molecules either joined to
form amylose or amylopectin. Found
in plants

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41
Q

Describe amylose

A
• Found in plants 
• Alpha glucose
• Glycosidic bonds between C1 
andC4
• Coils into a spiral shape held 
together by hydrogen bonds 
• OH groups on C2 inside of the 
coil, making the molecule less 
soluble and allowing hydrogen 
bonds to form to maintain the 
coil’s structure
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42
Q

Describe amylopectin

A
• Found in plants
• Alpha glucose
• Has glycosidic bonds between C1 
and C4, and also has branches 
formed by glycosidic bonds 
between C1 and C6 
• Coils into a spiral shape held 
together by hydrogen bonds, but 
with branches coming out of the 
spiral
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43
Q

What is glycogen?

A

A branched polysaccharide formed
from alpha glucose. A chemical
energy store in animal cells

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44
Q

Describe glycogen

A
• Found in animals 
• Like amylopectin with glycosidic 
bonds between C1 and C4, and 
branches formed by glycosidic 
bonds between C1 and C6
• The C1 C4 bonded chains are 
smaller than in amylopectin so 
glycogen has less tendency to coil
• Has more branches than 
amylopectin making it more 
compact
• Easier to remove monomer units 
as there are more ends
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45
Q

How do beta-glucose
molecules react with each
other?

A
• The OH groups on C1 and C4 are 
to far away to react, so each 
alternate beta glucose molecule 
must be turned upside down to 
reach 
• It is unable to could or form 
branches
• A straight chain molecule called 
cellulose is formed
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46
Q

Describe cellulose

A
• Cellulose molecules make 
hydrogen bonds with each other 
forming microfibrils
• Microfibrils join together to form 
macrofibrils that combine to 
produce fibres 
• The fibres are strong and insoluble 
and are used to make cell walls
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47
Q

Why is cellulose a good

material for cell walls?

A
Microfibrils and macrofibrils have 
very high tensile strength because 
of the glycosidic bonds and 
hydrogen bonds
• macrofibrils run in all directions, 
criss-crossing the wall for extra 
strength 
• Space between macrofibrils for 
water and mineral ions to pass in 
and out of the cell, making the cell 
wall full permeable
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48
Q

What are lipids?

A
Non-polar macromolecules contains 
the elements carbon, hydrogen and 
oxygen. Soluble in alcohol rather 
than water. Include triglycerides, 
phospholipids and sterols
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49
Q

Formation of a triglyceride

A
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50
Q

What are triglycerides?

A
Lipids composed of one glycerol 
(C3H8O3) molecule and three fatty 
acids. Fatty acids are carboxylic 
acids that consist of a carboxyl 
group (-COOH) which a hydrocarbon 
chain attached.
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51
Q

How are triglycerides formed?

A
• The hydroxyl groups in the fatty 
acid molecule and glycerol 
molecule react 
• This leads to the formation of 3 
water molecules and bonds 
between the fatty acid and 
glycerol molecule
• The bonds are called ester bonds, 
and the reaction is called 
esterification
• Esterification is an example of a 
condensation reaction
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52
Q

What is the difference between
saturated and unsaturated
triglycerides?

A
• Fatty acid chains that have no 
double bonds between the carbon 
atoms are saturated, and vice 
versa
• If there’s 1 double bond = 
monounsaturated
• If there’s 2 or more double bonds 
= polyunsaturated
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53
Q

How does the presence of
double bonds in unsaturated
triglycerides cause?

A
• Changes the bond angle and 
causes the molecule to kink or 
bend
• Therefore the molecules cannot 
pack so closely together
• Makes them liquid at rtp rather 
than solid, so they are oils rather 
than fats
54
Q

What type of triglycerides do

plants contain?

A

Unsaturated triglycerides, which

normally occur as oils

55
Q

Which type of triglycerides are

healthier?

A

Unsaturated triglycerides are
healthier for human than
triglycerides or (solid) fats

56
Q

What are phospholipids?

A

Modified triglycerides, where one
fatty acid has been replaced with a
phosphate group. They are found in
the cytoplasm of very cell

57
Q

Phospholipid

A
58
Q

What are the characteristics of

phospholipids?

A
• Have a non-polar end (the fatty 
acid chains) which are 
hydrophobic and repelled by water
• Have a charged head (the 
phosphate PO43-) which are 
hydrophilic and attracted to water
59
Q

How do phospholipids interact

with water?

A

When phospholipids are mixed with water, they form a phospholipid bilayer or double layer due to their amphipathic nature. The polar hydrophilic head group will interact with water to form hydrogen bonds with water but the two hydrophobic tails made of non-polar hydrocarbon tails repel water

60
Q

How do the characteristics of
phospholipids help in the
formation of cell membranes?

A
• The bilayer arrangement means 
that they can separate the aqueous 
environment in which cells usually 
exist, from the aqueous cytosol 
within the cells
61
Q

What are sterols?

A

Steroid alcohols. Complex alcohol
molecules based on a 4 carbon ring
structure with a hydroxyl (OH) group
at one end

62
Q

Describe the characteristics of

sterols

A
Have a dual hydrophilic/hydrophobic 
characteristics. The hydroxyl group 
is polar and therefore hydrophilic, 
and the rest of the molecule is 
hydrophobic.
63
Q

What is cholesterol?

A
• A type of sterol 
• The body primarily manufactures it 
in the liver and intestines 
• Vitamin D, steroid hormones and 
bile are all manufactured using 
cholestero
64
Q

What is the importance of
cholesterol in the formation of
cell membranes?

A
Positioned between the 
phospholipids with the hydroxyl 
group at the periphery of the 
membrane
• Adds to the stability of cell 
membranes
65
Q

What is the importance of
cholesterol in regulating the
fluidity of cell membranes?

A

Keeps membranes fluid at low
temperatures and stops them
becoming too fluid at high
temperatures

66
Q

What are the roles of lipids?

Due to their non-polar nature

A
• Membrane formation and the 
creation of hydrophobic barriers 
• Hormone production
• Electrical insulation necessary for 
impulse transmission 
• Waterproofing, e.g. in birds’ 
feathers and on plant leaves
67
Q

What are the roles of

triglycerides in particular

A
• Long-term energy storage 
Stored under the skin and around 
vital organs where they provide:
• Thermal insulation to reduce heat 
loss, e.g. in penguins
• Cushioning to protect vital organs 
e.g. heart and kidneys
• Buoyancy for aquatic animals like 
whales
68
Q

Define the following:

  1. Proteins
  2. Peptides
  3. Peptide bond
  4. Amino acid
A
1. One or more polypeptides 
arranged as a complex 
macromolecule 
2. Chains of two or more amino 
acid molecules 
3. Bond formed between two 
amino acids
4. Monomer used to build 
polypeptides and thus proteins
69
Q

Amino acid

A
70
Q

Describe what happens when

two amino acids react together

A
• The hydroxyl in the carboxylic acid 
group of one amino acid reacts 
with a hydrogen in the amine 
group of another amino acid 
• A peptide bond is formed between 
the amino acids and water is 
produced (condensation reaction)
• The resulting compound is a 
dipeptide
71
Q

When is a polypeptide formed?

A
• When many amino acids are joined 
together by peptide bonds
• This reaction sis catalysed by the 
enzyme peptide transferase 
present in ribosomes, the sites of 
protein synthesis
72
Q

What happens to the R-groups
of the amino acids when the
amino acids react?

A
• Different R-groups interact with 
each other (R-group interactions) 
forming different types of bond
• These bonds lead to polypeptides 
folding into complex structures 
(proteins)
73
Q

What does the presence of
different sequences of amino
acids lead to?

A
Different structures with different 
shapes being produced
The very specific shapes of proteins 
are vital for the many functions 
proteins have within living organisms
74
Q

What is the primary structure

of proteins?

A
• The sequence in which the amino 
acids are joined 
• Directed by information carried 
within DNA
• The amino acids in the sequence 
will influence how the 
polypeptide’s fold to give the 
proteins final shape, and 
determine its function
• The only bonds here are peptide 
bonds
75
Q

What is the secondary

structure of proteins?

A
• The oxygen, hydrogen, and 
nitrogen atoms of the amino acids 
(excluding R groups) interact
• A result of hydrogen bonds and 
forms at regions along long protein 
molecules depending on the 
amino sequences
76
Q

What are the two types of

secondary structure?

A
• Alpha Helix - Hydrogen bonds 
form within the amino acid chain, 
pulling it into a coil shape called 
an alpha-helix 
• Beta Pleated Sheet - Polypeptide 
bonds lie parallel to each other 
joined by hydrogen bonds, forming 
sheet-like structures.The pattern 
formed by individual amino acids 
makes the structure appear 
pleated
77
Q

What is tertiary structure?

A
• The folding of a protein into its 
final shape 
• Often includes sections of 
secondary structure
• The coiling or folding of sections 
of proteins into their secondary 
structures brings R-groups of 
different amino acids closer 
together so they can interact
78
Q

List the interactions that occur

between R-group

A
Hydrophobic and 
hydrophilicinteractioncs - weak 
interactions between polar and 
non-polar R-groups
• Hydrogen bonds - these are the 
weakest of bonds formed
• Ionic bonds - stronger than 
hydrogen bonds and form 
between oppositely charged Rgroups
• Disulfide bonds/bridges - covalent 
and the strongest of the bonds but 
only form between R-groups that 
contain sulphur atoms
79
Q

What is quaternary structure?

A
• Protein structure where a protein 
consists of more than 1 
polypeptide chain, e.g insulin has 
a quaternary structure
• Results from the association of 2 
or more individual proteins called 
subunits
• The interaction between subunits 
are the same as in tertiary 
structure except between different 
protein molecules rather than 
within one molecule 
• The protein subunits can be 
identical or different
80
Q

Describe hydrophilic and
hydrophobic interactions in
proteins

A
• Proteins are assembled in the 
aqueous environment of the 
cytoplasm
• The way a protein will fold also 
depends on whether the R-groups 
are hydrophilic or hydrophobic 
• Hydrophilic groups arena the 
outside, whilst hydrophobic are on 
the inside of the molecule (away 
from the cytoplasm
81
Q

List the types of proteins

A
  • Globular proteins
  • Conjugated proteins
  • Fibrous proteins
82
Q

What are globular proteins?

A
Compact, spherical, water-soluble 
proteins
• Form when proteins fold into their 
tertiary structures so that the 
hydrophobic R-groups on the 
amino acid are kept away from the 
aqueous environment 
• Hydrophilic R-groups on the 
outside of the protein meaning the 
proteins are soluble in water
• e.g. Insulin
83
Q

Describe how the structure of

Insulin is suited to its function

A
• Globular protein 
• Hormone involved in regulation of 
blood glucose concentration
• Hormones are transported in the 
bloodstream so need to soluble
• Hormones have to fit into specific 
receptor on cell-surface 
membranes to work, therefore 
need to have precise shapes
84
Q

What are conjugated proteins?

A
Globular proteins that contain a 
prosthetic group.
Lipids or carbohydrates can 
combine with proteins forming 
lipoproteins or glycoproteins. Metal 
ions and molecules derived from 
vitamins also form prosthetic groups
• e.g. Haemoglobin and Catalase 
both contain prosthetic harm groups 
(Fe2+)
85
Q

Describe how the structure of
haemoglobin makes it suited
to its function

A
Red, oxygen-carrying pigment in 
red blood cells
• Quaternary protein made from 4 
polypeptides (2 alpha and 2 beta 
subunits)
• Each subunit contains a prosthetic 
hem group
• The Fe2+ ions in the haem groups 
are each able to combine 
reversibly with an oxygen molecule 
which enables haemoglobin to 
transport oxygen around the body
86
Q

Describe how the structure of
catalase makes it suited to its
function

A
• An enzyme 
• A quaternary protein containing 4 
prosthetic harm groups 
• The presence of Fe2+ ions in the 
haem groups allow catalase to 
interact with hydrogen peroxide 
and speed up its breakdown
• Hydrogen peroxide is a common 
byproduct of metabolism but 
damaging to cells and cell 
components, so catalase makes 
sure it doesn’t accumulate
87
Q

What are fibrous proteins?

A
Long insoluble, structural proteins
• Due to the presence of a high 
proportion of amino acids with 
hydrophobic R-groups in their 
primary structures 
• Amino acid sequence in primary 
structure is usually very repetitive 
leading to very organised 
structures 
• Are NOT folded into complex 3D 
shapes like globular proteins
• E.g. Keratin, Elastin and Collagen
88
Q

Describe how the structure of

keratin is suited to its function

A
• Group of fibrous proteins 
presenting hair, skin and nails 
• Large proportion of the sulfurcontaining amino acid cysteine 
leading to many strong disulphide 
bonds forming strong, inflexible, 
insoluble materials 
• Hair contains fewer disulphide 
bonds than nails, so is more 
flexible
89
Q

Describe how the structure of

elastin is suited to its function

A
• Fibrous protein found in elastic 
fibres
• Elastic fibres are present in the 
walls of blood vessels and in the 
alveoli of the lungs 
• Give these structures flexibility to 
expand when needed but also to 
return to their normal size
• Quaternary protein made from 
many stretch molecules called 
tropoelastin
90
Q

Describe how the structure of
collagen makes it suited to its
function

A
• Fibrous protein
• Connective tissue found in skin, 
tendons, ligaments and the 
nervous systems
• Many different forms but all are 
made up of 3 polypeptides wound 
together in a long and strong ropelike structure
• Like rope, collagen has flexibility
91
Q

Describe the test for starch

A
1. Add iodine solution (in 
potassium iodide) to a sample
2. If starch is present, you will see a 
colour change from yellowbrown to blueback 
• When dissolved in potassium 
iodide, the iodine (I2) forms a 
triiodide I3-, which slips into the 
middle of the amylose helix, 
causing a colour change
92
Q

Describe the test for reducing
sugars (all monosaccharides
and some disaccharides)

A
  1. Place the sample in a boiling
    tube. If its not liquid, grind it up
    or lend it in water
  2. Add an equal volume fo
    Benedict’s solution
  3. Heat the mixture gently in a
    boiling water bath for 5 minutes
    Blue > Green > Yellow > Orange >
    Red
    • Benedict’s reagent is an alkaline
    solution of copper (II) sulphate
    • The more reducing sugar present,
    the more brick-red precipitate
    formed and the less blue Cu2+
    ions left in solution
93
Q

Describe the test for nonreducing sugars

A
1. Do Benedict’s test for reducing 
sugars, the result will be 
negative 
2. Sucrose is the most common 
non-reducing sugar
3. If sucrose is first boiled with 
dilute hydrochloric acid then it’ll 
give a positive result when 
warmed with Benedict’s solution
• This is because the sucrose has 
been hydrolysed by the acid to 
glucose and fructose, both 
reducing sugars
94
Q

Describe the test for lipids

A
  1. Mix the sample with ethanol
  2. The resulting solution is mixed
    with water and shaken
  3. If a white emulsion forms as a
    layer on top the solution, this
    indicated the presence of a lipid
  4. If the solution remains clear, the
    test is negative
95
Q

Describe the test for proteins

A
1. Add Biuret A (sodium hydroxide) 
and then Biuret B (copper 
sulphate) to the sample 
2. If a protein is present, the colour 
changes from light blue to lilac/ 
mauve
96
Q

What are nucleic acids?

A

Large polymers formed from
nucleotides. Contain the elements
carbon, nitrogen, hydrogen,
phosphorus, and oxygen

97
Q

Describe the composition of

nucleotides

A
• A pentose monosaccharide 
containing 5 carbon atoms 
• A phosphate group, (PO42-) and 
inorganic molecule that is acidic 
and negatively charged
• A nitrogenous base - a complex 
organic molecule containing 1 or 2 
carbon rings in its structure, as 
well as nitrogen
98
Q

How do nucleotides link
together to form a
polynucleotide?

A
By condensation reactions
• Phosphate group at the 5th carbon 
of the pentose sugar (5’) of one 
nucleotide forms a covalent bond 
with the hydroxyl (OH) group at the 
3rd carbon (3’) of the pentose 
sugar of another nucleotide
• These bonds are called 
phosphodiester bonds
• Forms a long, strong sugarphosphate ‘backbone’ 
• Phosphodiester bonds are broken 
by hydrolysis
99
Q

What is Deoxyribonucleic acid

(DNA) ?

A
The molecule responsible for the 
storage of genetic information 
• The sugar is deoxyribose, which 
has 1 less oxygen atoms than a 
ribose sugar
• The nucleotides each have 1 of 4 
different bases: Adenide, Thymine, 
Guanine, or Cytosine
100
Q

What are pyrimidines?

A

• Single-ringed, nitrogenous bases
that form part of a nucleotide
• Smaller bases
• Thymine (T) and Cytosine (C

101
Q

What are purines?

A

• Double-ringed, nitrogenous bases
that form part of a nucleotide
• Larger bases
• Adenine (A) and Guanine (G

102
Q

Describe the double helix

structure of DNA

A
Made up of 2 strands of 
polynucleotides coiled into a helix 
• The 2 strands are held together by 
hydrogen bonds between the 
bases 
• Each strand has a phosphate 
group (5’) at one end, and a 
hydroxyl group (3’)at the other end
• The 2 parallel strands run in 
opposite directions - antiparallel
103
Q

What is complementary base

pairing?

A
Specific hydrogen bonding between 
nucleic acid bases. A binds to T or 
U, C binds to G
• A and T form 2 hydrogen bonds so 
always join with each other 
• C and G form 3 hydrogen bonds 
so always join with each other
104
Q

What are the consequences of

complimentary base pairing?

A
• A small pyrimidine base always 
binds to a larger purine base; this 
arrangement keeps a constant 
distance between the DNA 
backbones, resulting in parallel 
polynucleotide chains
• DNA always has equal amounts of 
adenine and thymine, and cytosine 
and guanine
105
Q

What is Ribonucleic acid?

(RNA

A
Polynucleotide molecules involved in 
the copying and transfer of genetic 
information from DNA. 
The monomers are nucleotides 
consisting of a ribose sugar and 1 of 
four bases: Adenine, Uracil, 
Cytosine, or Guanine
106
Q

What are the similarities and
differences between DNA and
RNA?

A
Similarities:
• RNA nucleotides form polymers in 
the same way as DNA nucleotides 
- by the formation of 
phosphodiester bonds
Differences:
• In RNA the pentose sugar is 
ribose, meanwhile in DNA it’s 
deoxyribose 
• In RNA, the thymine base is 
replaced with Uracil
107
Q

What is DNA replication?

A

The semi-conservative process of
the production of identical copies of
DNA molecules

108
Q

What is semi-conservative

replication?

A

DNA replication results in one old
strand and one new strand present
in each daughter DNA molecules

109
Q

Describe the process of semiconservative replicatio

A
1. The enzyme DNA helicase 
travels along the DNA backbone, 
catalysing reactions that breaks 
the hydrogen bonds between 
complimentary base pairs 
2. After the ‘unzipping’, free DNA 
nucleotides will then pair with 
their complimentary bases, 
which have been exposed as the 
strands separate 
3. Hydrogen bonds are formed 
between the new complimentary 
bases
4. The enzyme DNA polymerase 
catalyses the formation of 
phosphodiester bonds between 
adjacent new nucleotides
110
Q

What is a mutation?

A
A change in the genetic material 
which may affect the phenotype of 
the organism.
Happen due to random error in the 
replication of DNA that lead to a 
change in the sequence of bases
111
Q

What is the genetic code?

A

The sequences of baes in DNA are
the ‘instructions’ for the sequences
of amino acids in the production of
proteins

112
Q

What is a triplet code?

A
The genetic code is a sequence of 
three nucleic acids bases, called a 
codon. Each codon codes for one 
amino acids.
A section of DNA that contains the 
complete sequence of baes 
(codons) to ode for an entire protein 
is called a gene
113
Q

What is a triplet code?

A
The genetic code is a sequence of 
three nucleic acids bases, called a 
codon. Each codon codes for one 
amino acids.
A section of DNA that contains the 
complete sequence of baes 
(codons) to ode for an entire protein 
is called a gene
114
Q

Why is the genetic code a

degenerate code?

A
• There are 64 different base triplets 
or codons possible, but there are 
only 20 amino acids
• Therefore, many amino acids can 
be coded for by more than one 
codon
115
Q

How are genes read?

A
• There’s a start codon (ATG) that 
signals the start of a sequence 
that codes for a protein (if it’s in 
the middle of a gene it codes for 
methionine) 
• Having a start codon means that 
codons are read ‘in frame’, so the 
genetic code is non-overlapping
• There are 3 stop codons that don’t 
code for any amino acids, and 
signal the end of the sequence
116
Q

What is transcription?

A
The process of copying smaller 
sections of DNA base sequence to 
produce smaller molecules of 
mRNA, which can be transported 
out of the nucleus via the nuclear 
pores, to the site of protein 
synthesis
117
Q

Describe the process of

transcription

A
1. A gene unwinds and unzips, 
aided by DNA helicase, and the 
hydrogen bonds between 
complimentary nucleotide bases 
break
2. The sense strand (5’ to 3’) codes 
for the protein, whilst the 
antisense strand (3’ to 5’)acts as 
the template strand during 
transcription 
3. RNA polymerase catalyses the 
formation of temporary hydrogen 
bonds between RNA nucleotides 
and their complimentary DNA 
bases on the template strand 
4. The strand of RNA produced is 
complimentary to the template 
strand, so is a copy of the 
sense/ coding strand
5. Messenger RNA (mRNA) passes 
out of the nucleus, through the 
nuclear envelope, whilst the DNA 
double helix reforms
118
Q

What are ribosomes made up

of? (eukaryotic cells)

A

2 subunits, one large and one
small
• Almost equal amounts of protein
and ribosomal RNA (rRNA)

119
Q

What is the role of rRNA?

A

• Maintaining the structural stability
of the protein synthesis sequence
• Biochemical role in catalysing the
reaction

120
Q

What happens to mRNA after it

has left the nucleus?

A
• Binds to a specific site on the 
small subunit of a ribosome 
• The ribosome holds mRNA in 
position while it is translated into a 
sequence of amino acids 
• This process is called translation
121
Q

What is translation?

A
The process by which the 
complementary code carried by 
mRNA is decoded by tRNA into 
sequence of amino acids. This 
occurs at a ribosome
122
Q

What is transfer RNA (tRNA)?

A
Form of RNA that carries an amino 
acid specific to its anticodon to the 
correct position along mRNA during 
translation
• Single stranded polynucleotides, 
but can twist into a hairpin shape
• At one end is a trio of nucleotide 
bases that recognises and 
attaches to a specific amino acid
• At the loop is another triplet of 
bases called an anticodon that is 
complementary to a specific 
codon of bases on the mRNA
123
Q

Describe how translation

happens at a ribosome

A
1. mRNA binds to the small subunit 
of the ribosome at its start 
codon (AUG)
2. A tRNA with the complementary 
anticodon (UAC) binds to the 
mRNA start codon. This tRNA 
carries the amino acid 
methionine 
3. Another tRNA with the 
complementary anticodon, and 
carrying an amino acid, binds to 
the next codon on the mRNA. A 
maximum of 2 tRNAs can be 
bound at the same time
4. The 1st amino acid (methionine) 
is transferred to the amino acid 
on the 2nd tRNA by the 
formation of a peptide bond. 
This is catalysed by the enzyme 
peptidyl transferase, which is an 
rRNA component of the 
ribosome 
5. The ribosome then moves along 
the mRNA, releasing the 1st 
tRNA. The 2nd tRNA becomes 
the 1st 
6. Stages 3-5 are repeated until the 
ribosome reaches the end of the 
mRNA at a stop codon, and the 
polypeptide is released
124
Q

What is ATP?

A
Adenosine triphosphate
A nucleotide composed of a 
nitrogenous adenine base, a 
pentose sugar, and 3 phosphate 
groups. The ‘universal energy 
currency’ for cells, because it is 
used for energy transfer in all cells.
125
Q

What are the 3 main types of
activity cells require energy
for?

A
• Synthesis - e.g. of large molecules 
such as proteins
• Transport - e.g. pumping 
molecules or ions across cell 
membranes by active transport 
• Movement - e.g. protein fibres in 
muscle cells that cause muscle 
contraction
126
Q

What is ADP?

A
Adenosine diphosphate
A nucleotide composed of a 
nitrogenous adenine base, a 
pentose sugar and 2 phosphate 
groups
Formed by the hydrolysis of ATP, 
releasing a phosphate ion and 
energy
127
Q

Why is ATP not a good longterm energy sto

A
• The instability of the phosphate 
bonds 
• Fats and carbohydrates are better 
long-term energy stores 
• Energy released in the breakdown 
of these molecules (a process 
called cellular respiration) is used 
to create ATP 
• A phosphate group is reattached 
to an ADP molecule 
(phosphorylation which is an 
example of a condensation 
reaction)
128
Q

Why do cells not store large

amounts of ATP?

A
• Due to the instability of ATP
• Instead ATP is rapidly reformed by 
the phosphorylation of ADP 
• Interconversion of ATP and ADP is 
happening constantly in all living 
cells, so cells don’t need a large 
store of ATP
• ATPis a good immediate energy 
store
129
Q

How does ATP carry energy?

A
1. When a cell needs energy, ATP is 
broken down to ADP and Pi
2. In the hydrolysis reaction, a 
phosphate bond is broken and 
energy released to be catalysed 
by the enzyme ATP hydrolase
3. ATP hydrolysis can be couple to 
other reactions in the cell - the 
energy can be used directly to 
make the coupled reaction 
happen (instead of being lost as 
heat)
4. The released phosphate can be 
added to another compound 
(phosphorylation) which often 
makes the compound more 
reactive
5. ATP can be re-synthesised in a 
condensation reaction between 
ADP and Pi. The enzyme ATP 
synthase catalyses it during both 
respiration and photosynthesis
130
Q

What are the properties of ATP
that make it suited to carry out
its function in energy transfer?

A
• Small - moves easily into, out of, 
and within cells 
• Water soluble - energy requiring 
processes happen in aqueous 
environments
• Contains bonds between 
phosphates with immediate 
energy: large enough to be useful 
for cellular reactions, but not so 
large that energy is wasted as heat
• Releases energy in small quantities 
- quantities are suitable to most 
cellular needs, so that energy is 
not wasted as heat
• Easily regenerated - can be 
recharged with energy