Flashcards - Topic 2 Biological Molecules - CAIE Biology A-Level (2019-2021 Syllabus)

CAIE Biology A-level
Topic 2: Biological Molecules

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Outline the Benedict’s test for reducing
sugars
Outline the Benedict’s test for reducing sugars.
1. Add an equal volume of Benedict’s reagent to the

sample to be test.
2. Heat the mixture in a water bath at 100°C for 5
minutes.
3. Positive result: colour change from blue to green to
yellow to orange to brick-red. Precipitate forms.
Outline the Benedict’s test for
non-reducing sugars
Outline the Benedict’s test for non-reducing sugars
1. Reducing sugar test, negative result, reagent remains blue.
2. Hydrolyse non-reducing sugars (e.g. sucrose) into their
monomers by adding an equal volume of HCl.
3. Heat in a boiling water bath for 5 minutes.
4. Neutralise the mixture using sodium hydrogen carbonate
solution.
5. Proceed with the Benedict’s test as usual.
How can the Benedict's test be made
more quantitative?
How can the Benedict's test be made more quantitative?
Either:
Measure the time from immersing solution in water bath till

the first colour change is produced
Or:
Create standard solutions of known concentrations, and

compare colour change to estimate concentration
Outline the Biuret test for proteins
Outline the Biuret test for proteins.
1. Add an equal volume of sodium hydroxide to a sample at room

temperature.
2. Add a few drops of dilute copper (II) sulfate solution. Swirl to mix.
(steps 1 & 2 make the Biuret reagent)
3. Positive result: colour change from pale blue to violet.

Negative result: solution remains blue.
Describe how to test for and measure
the presence of starch in a sample
Describe how to test for and measure the presence
of starch in a sample.
1. Add iodine solution.
2. Positive result: colour changes from yellow-brown to blue-black.
Describe the emulsion test for fats
and oils
Describe the emulsion test for fats and oils.
● Add ethanol to the sample and shake.

● Allow the mixture to settle.
● Add an equal volume of water.
● Record any observations.
Describe the positive result of an
emulsion test
Describe the positive result of an emulsion test.
White, cloudy emulsion forms.
Define ‘monomer’
Define ‘monomer’.
A single subunit that is used to build

larger polymers.
Define ‘polymer’
Define ‘polymer’
A large molecule comprised of repeating

subunits (monomers), often formed by
condensation reactions.
Define ‘macromolecule’
Define ‘macromolecule’
A large biological molecule.
Define ‘monosaccharide’, ‘disaccharide’,
‘polysaccharide’
Define 1. monosaccharide, 2. disaccharide, 3.
polysaccharide
1. A single unit of carbohydrate.
2. 2 units of carbohydrate joined by condensation,
held by a glycosidic bond.
3. A polymer with monomers of monosaccharides
joined by condensation reactions, held by
glycosidic bonds.
Describe the structure of 𝛂 and β glucose
Describe the structure of 𝛂 and β glucose
Both are hexose

monosaccharides (6C)
with a ring structure.
𝛂 glucose ꞵ glucose
What is the difference between 𝛂 and β glucose?
What is the difference between 𝛂 and β glucose?
The OH group on carbon 1 for alpha

glucose is below the plane, while that for
beta glucose is above the plane
What happens in condensation
reactions- with reference to glycosidic
bonds?
What happens in condensation reactions?
A chemical bond forms between two molecules and a molecule of water is
produced. H is removed from one molecule, OH from another.
When this occurs between carbohydrates, it is referred to as a glycosidic

bond. This is a type of covalent bond.
State how sucrose is formed via the
formation of a glycosidic bond.
State how sucrose is formed via the formation of a glycosidic bond.
𝛂 glucose and ꞵ fructose form sucrose via the

omission of H2O (condensation) forming a glycosidic
bond between them.
How are glycosidic bonds broken? What
is this known as?
How are glycosidic bonds broken? What is this known as?
Water is used to break the glycosidic bond. This is known as a hydrolysis

reaction- consider the meaning behind the term “hydrolysis”.
Link- we added HCl to test for non-reducing sugars to hydrolyse their

poly- or di-saccharides.
Describe the structures of amylose and amylopectin
Describe the structures of amylose and amylopectin
● Amylose: 1,4-glycosidic bonds, unbranched
helical.
● Amylopectin: 1-4 & 1,6-glycosidic bonds,
branched.
How do the structures of amylose and
amylopectin relate to their function?
How do the structures of amylose and amylopectin relate to their
function?
Amylose and amylopectin (starch) act as a storage polymer of 𝛼-glucose
in plant cells:
● insoluble = no osmotic effect on cells.
● large = does not diffuse out of cells.
Amylose: Amylopectin:
● 1,4 & 1,6 glycosidic bonds.
● 1,4 glycosidic bonds.
● branched = many terminal ends
● Unbranched helix = compact to for rapid hydrolysis into glucose.
store lots of energy.
Describe the structure and functions of
glycogen
Describe the structure and functions of glycogen
Main storage polymer of 𝛼-glucose in animal cells (but also
found in plant cells):
● 1,4 & 1,6 glycosidic bonds.
● Branched (more so than amylopectin) = many terminal
ends for hydrolysis.
● Insoluble = no osmotic effect & does not diffuse out of
cells.
● Large but compact for maximum energy storage.
Describe the structure and functions of
cellulose
Describe the structure and functions of cellulose.
Polymer of 𝛽-glucose (polysaccharide) gives rigidity to plant cell
walls (prevents bursting under turgor pressure, holds stem up).
● 1,4 glycosidic bonds.

● Straight-chain, unbranched molecule.
● Alternate glucose molecules are rotated 180°.
● H-bond crosslinks between parallel strands form microfibrils =
high tensile strength.
Describe the structure of a triglyceride-
with reference to how it is formed
Describe the structure of a triglyceride- with reference to how
it is formed
One molecule of glycerol forms ester bonds with three fatty acids
via condensation reactions.
Image source: OpenStax College, CC BY 3.0
Relate the structure of triglycerides to
their functions
Relate the structure of triglycerides to their functions
● High energy-to-mass ratio - energy storage.
● Insoluble hydrocarbon chain - no effect on water potential of cells,

used for waterproofing.
● Slow conductor of heat - thermal insulation.
● Less dense than water - buoyancy of aquatic animals.

● Protects organs- high melting point- very stable molecule resistant to
large amounts of force.
Describe the structure and function of phospholipids
Describe the structure and function of phospholipids
Polar molecule: glycerol backbone attached to 2
hydrophobic fatty acid tails and 1 hydrophilic polar
phosphate head.
● Forms phospholipid bilayer in water - component of

membranes: the hydrophobic the tails allow for control
over the movement of water-soluble molecules in and
out of cells.
Describe the common structure of an
amino acid
Describe is the common structure of an amino acid
● Amine group (-NH2).

● Variable side chain (R).
● Carboxyl group (-COOH).
● H atom.
How are peptide bonds formed?
How are peptide bonds formed?
The OH is lost from the carboxyl group,
and an H lost from the amine group
(condensation reaction), forming a peptide
bond (-CONH-).
Describe and name the process by
which peptide bonds are broken
Describe and name the process by which peptide bonds are
broken
H2O is split to H + OH, OH returns to the

carboxyl group, H to the amine - this is a
hydrolysis reaction.
What is the primary structure of a
protein?
What is the primary structure of a protein?
A sequence of amino acids in a

polypeptide, held by peptide bonds.
What is secondary structure?
What is secondary structure?
The regular folding of a polypeptide into

alpha helices and beta pleated sheets,
held together by hydrogen bonds.
What is tertiary structure?
What is tertiary structure?
The further coiling of a protein into its

functional 3D shape. Held by hydrogen,
ionic, and disulphide bonds, and
hydrophobic interactions.
What is quaternary structure?
What is quaternary structure?
The folding of 2 or more polypeptides
into a 3D shape, which may include
prosthetic (non-protein) groups. Held by
hydrogen, ionic, and disulphide bonds,
and hydrophobic interactions.
Describe the structure of haemoglobin
Describe the structure of haemoglobin
● Globular conjugated protein with prosthetic group.
● 2 𝛼-chains, 2 𝛽-chains, 4 prosthetic haem groups.
● Water-soluble so dissolves in plasma.
● Fe2+ haem group forms coordinate bond with O2.
● Tertiary structure changes so it is easier for subsequent
O2 molecules to bind (cooperative binding).
State the features of a globular protein -
with reference to haemoglobin
State the features of a globular protein - with reference to haemoglobin
● Spherical & compact.

● Hydrophilic R groups face outwards & hydrophobic R groups
face inwards = usually water-soluble.
● Involved in metabolic processes e.g. enzymes such as
amylase, insulin (2 polypeptide chains linked by 2 disulfide
bonds), haemoglobin.
● Compact nature means haemoglobin can transport more
oxygen per unit of blood.
Describe the structure and function of globular
proteins
Describe the structure and function of globular
proteins
● Spherical & compact.
● Hydrophilic R groups face outwards & hydrophobic
R groups face inwards = usually water-soluble.
● Involved in metabolic processes e.g. enzymes such
as amylase, insulin (2 polypeptide chains linked by 2
disulfide bonds), haemoglobin.
Describe the structure of collagen
Describe the structure of collagen
Fibrous: insoluble, long strands with high tensile strength.
Made up of 3 polypeptide chains coiled to form a triple helix.
Every third amino acid is glycine (the smallest amino acid).
Collagen molecules lie parallel to form collagen strands, held
by staggered covalent cross bridges between lysine residues.
How does hydrogen bonding occur in
water?
How does hydrogen bonding occur in water?
The 𝛿+ hydrogen on one water molecule

is attracted to the lone pair of the 𝛿-
oxygen on another water molecule.
What are the properties of water due to
hydrogen bonding?
What are the properties of water due to hydrogen bonding?
High surface tension.
Acts as a solvent for water soluble molecules so can act as a transport
medium.
High specific heat capacity.
High latent heat of vaporisation.
Higher boiling point than expected (liquid at room temperature).
Ice is less dense than liquid water.

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CAIE Biology A-level

Topic 2: Biological Molecules

PMT Education is licensed under https://bit.ly/pmt-cc

1. Add an equal volume of Benedict’s reagent to the

Measure the time from immersing solution in water bath till

Create standard solutions of known concentrations, and

1. Add an equal volume of sodium hydroxide to a sample at room

3. Positive result: colour change from pale blue to violet.

2. Positive result: colour changes from yellow-brown to blue-black.

● Add ethanol to the sample and shake.

White, cloudy emulsion forms.

A single subunit that is used to build

A large molecule comprised of repeating

A large biological molecule.

Both are hexose

The OH group on carbon 1 for alpha

When this occurs between carbohydrates, it is referred to as a glycosidic

𝛂 glucose and ꞵ fructose form sucrose via the

Water is used to break the glycosidic bond. This is known as a hydrolysis

Link- we added HCl to test for non-reducing sugars to hydrolyse their

● 1,4 glycosidic bonds.

Image source: OpenStax College, CC BY 3.0

● High energy-to-mass ratio - energy storage.

● Insoluble hydrocarbon chain - no effect on water potential of cells,

● Slow conductor of heat - thermal insulation.

● Less dense than water - buoyancy of aquatic animals.

● Forms phospholipid bilayer in water - component of

● Amine group (-NH2).

H2O is split to H + OH, OH returns to the

A sequence of amino acids in a

The regular folding of a polypeptide into

The further coiling of a protein into its

● Spherical & compact.

The 𝛿+ hydrogen on one water molecule

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