NAME: __________________
Module 2: Foundations in
biology
2.1.2 Biological molecules
Specification points
Mastery comes from retrieving knowledge regularly, making links between
concepts and consolidation.
Specification points:
(a) how hydrogen bonding occurs between
water molecules, and relate this, and other
properties of water, to the roles of water for
living organisms
(b) the concept of monomers and polymers and
the importance of condensation and hydrolysis
reactions in a range of biological molecules
(c) the chemical elements that make up
biological molecules
(d) the ring structure and properties of glucose
as an example of a hexose monosaccharide and
the structure of ribose as an example of a
pentose monosaccharide
(e) the synthesis and breakdown of a
disaccharide and polysaccharide by the
formation and breakage of glycosidic bonds
(f) the structure of starch (amylose and
amylopectin), glycogen and cellulose molecules
(g) how the structures and properties of
glucose, starch, glycogen and cellulose
molecules relate to their functions in living
organisms
(h) the structure of a triglyceride and a
phospholipid as examples of macromolecules
(i) the synthesis and breakdown of triglycerides
by the formation (esterification) and breakage
of ester bonds between fatty acids and glycerol
(j) how the properties of triglyceride,
phospholipid and cholesterol molecules relate
to their functions in living organisms
(k) the general structure of an amino acid
(l) the synthesis and breakdown of dipeptides
and polypeptides, by the formation and
breakage of peptide bonds
(m) the levels of protein structure
(n) the structure and function of globular
proteins including a conjugated protein
(o) the properties and functions of fibrous
proteins
(p) the key inorganic ions that are involved in
biological processes
q) how to carry out and interpret the results of
the following chemical tests:
•biuret test for proteins
•Benedict’s test for reducing and non-reducing
sugars
•reagent test strips for reducing sugars
•iodine test for starch
•emulsion test for lipids
(r) quantitative methods to determine the
concentration of a chemical substance in a
solution
(s) (i) the principles and uses of paper and thin
layer chromatography to separate biological
molecules / compounds
(ii) practical investigations to analyse biological
solutions using paper or thin layer
chromatography.
PAG6 (chromatography or electrophoresis),
PAG9 (Qualitative testing)
(a) Describe how hydrogen bonding occurs between water molecules, and relate this,
and other properties of water, to the roles of water for living organisms.
A range of roles that relate to the properties of water, including solvent, transport
medium, coolant and as a habitat AND roles illustrated using examples of prokaryotes
and eukaryotes.
(b) Describe the concept of monomers and polymers and explain the importance of
condensation and hydrolysis reactions in a range of biological molecules.
(c) Describe the chemical elements that make up biological molecules.
To include:
C, H and O for carbohydrates
C, H and O for lipids
C, H, O, N and S for proteins
C, H, O, N and P for nucleic acids.
(d) Describe the ring structure and properties of glucose as an example of a hexose
monosaccharide and the structure of ribose as an example of a pentose
monosaccharide.
To include the structural difference between an α- and a β-glucose molecule AND the
difference between a hexose and a pentose monosaccharide.
(e) the synthesis and breakdown of a disaccharide and polysaccharide by the formation
and breakage of glycosidic bonds.
(b) Describe the concept of monomers and polymers and explain the importance of
condensation and hydrolysis reactions in a range of biological molecules.
(f) Describe the structure of starch (amylose and amylopectin), glycogen and cellulose
molecules.
(g) Explain how the structures and properties of glucose, starch, glycogen and cellulose
molecules relate to their functions in living organisms.
(h) Describe the structure of a triglyceride and a phospholipid as examples of
macromolecules.
To include an outline of saturated and unsaturated fatty acids.
(i) Describe the synthesis and breakdown of triglycerides by the formation
(esterification) and breakage of ester bonds between fatty acids and glycerol.
(j) Explain how the properties of triglyceride, phospholipid and cholesterol molecules
relate to their functions in living organisms.
To include hydrophobic and hydrophilic regions and energy content AND illustrated
using examples of prokaryotes and eukaryotes.
(k) Describe the general structure of an amino acid.
(l) Describe the synthesis and breakdown of dipeptides and polypeptides, by the
formation and breakage of peptide bonds.
(m) Describe the levels of protein structure.
To include primary, secondary, tertiary and quaternary structure AND hydrogen
bonding, hydrophobic and hydrophilic interactions, disulfide bonds and ionic bonds.
(n) Describe the structure and function of globular proteins including a conjugated
protein.
To include haemoglobin as an example of a conjugated protein (globular protein with a
prosthetic group), a named enzyme and insulin.
(o) Describe the properties and functions of fibrous proteins.
To include collagen, keratin and elastin (no details of structure are required).
(p) Describe the key inorganic ions that are involved in biological processes.
To include the correct chemical symbols for the following cations and anions:
cations: calcium ions (Ca2+), sodium ions (Na+), potassium ions (K+), hydrogen ions
(H+), ammonium ions (NH4+)
anions: nitrate (NO3–), hydrogencarbonate (HCO3–), chloride (Cl –), phosphate
(PO43–), hydroxide, (OH–).
(q) Describe how to carry out and interpret the results of the following chemical tests:
•• biuret test for proteins •• Benedict’s test for reducing and non-reducing sugars
•• reagent test strips for reducing sugars •• iodine test for starch
•• emulsion test for lipids
(r) Describe quantitative methods to determine the concentration of a chemical
substance in a solution.
To include colorimetry and the use of biosensors (an outline only of the mechanism is
required).
(s) (i) Describe the principles and uses of paper and thin layer chromatography to
separate biological molecules / compounds.
(ii) Describe practical investigations to analyse biological solutions using paper or thin
layer chromatography.
For example the separation of proteins, carbohydrates, vitamins or nucleic acids.
Biological Molecules
1. The table below refers to the formula and structure of some biological molecules.
Complete the table by writing in the name, the formula or the structure of the molecule where appropriate in the
empty boxes.
Name Formula Structure
Water H2O
NH2RCHCOOH
Fatty acid
(Total 6 marks)
2. The table below refers to two organic molecules.
If the statement is correct for the molecule, place a tick (√) in the appropriate box. If it is incorrect, place a cross
(X) in the appropriate box.
(Total 5 marks)
3. The diagram below shows the structure of a lipid molecule.
(a) (i) Name the parts labelled A and B.
A ............................................................................................................
B ............................................................................................................
(2)
(ii) Name this type of lipid.
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(1)
(iii) Name the chemical reaction used to form the bonds between A and B.
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(1)
(b) (i) State one function of this type of lipid in living organisms.
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(1)
(ii) State one feature of the molecules of this type of lipid which makes them suitable for the function you have given.
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(1)
(Total 6 marks)
4. The diagram below shows a carbohydrate molecule formed from two glucose molecules.
(a) Name the molecule shown in the diagram.
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(1)
(b) What type of carbohydrate is this?
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(c) Name the type of bond labelled X on the diagram, that links the two glucose molecules.
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(1)
(d) Many glucose molecules can be linked together to form cellulose.
(i) State one function of cellulose in living organisms.
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(1)
(ii) Explain how the structure of cellulose is related to its functions.
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(2)
(Total 6 marks)
5. The table below refers to some disaccharides, their constituent monomers and their roles in living organisms.
Complete the table by writing in the appropriate word or words in the empty boxes.
Disaccharide Constituent monomers One role in living
organisms
Carbohydrate source in
Lactose
mammalian milk
Glucose + glucose
Form in which sugars
are transported in plants
(Total 5 marks)
6. (a) State two structural differences between the molecules of the polysaccharides cellulose and glycogen.
Cellulose Glycogen
1
2
(2)
(b) State two structural differences between the molecules of the proteins collagen and insulin.
Collagen Insulin
(2)
(Total 4 marks)
7. The statements in the table below refer to three polysaccharide molecules. If the statement is correct, place a
tick (√) in the appropriate box and if the statement is incorrect, place a cross ( x) in the appropriate box.
(Total 4 marks)
8. Read through the following passage about protein structure, then write on the dotted lines the most
appropriate word or words to complete the passage.
The tertiary structure of a protein depends on its primary and secondary structure.
The primary structure is the ………………………………….. of amino acids, which are joined together
by ………………………………….. bonds to form a chain. This type of bond is formed when a
………………………………….. reaction takes place between two amino acids.
The chain of amino acids may be folded into an alpha helix, held in shape by………………….. bonds.
A number of different types of bonds hold the tertiary and quaternary structure in shape. For example, the
two peptide chains in insulin are held together by ………………………………….. bonds which form
between the ………………………………….. of certain amino acids.
(Total 6 marks)
9. (a) Explain what is meant by the primary structure of a protein molecule.
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(2)
(b) Explain the role of hydrogen bonding in maintaining the structure of a globular protein such as insulin.
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(3)
(c) Describe how the structure of a fibrous protein, such as collagen, differs from the structure of a globular protein.
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(3)
(Total 8 marks)
10. Polypeptides are synthesised from amino acids. The diagram below shows the molecular structure of an
amino acid.
(a) (i) In the space below, draw a molecular diagram to show how this amino acid reacts with another amino
acid to produce a dipeptide.
(3)
(ii) Name the type of reaction involved.
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(1)
(b) State two functions of the R groups in a polypeptide chain.
1.........…………………………………………………………………..…………….……………………………
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2....................…………………………………………………………………..…………….……………………
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(2)
(Total 6 marks)
11. Read through the following account of the properties of water, then write on the dotted lines the most
appropriate word or words to complete the account.
Water has the chemical formula ………………………………… . Water molecules are
described as ………………………………….. because they have a slight positive charge
at one end of the molecule and a slight negative charge at the other end. As a result,
individual molecules form ………………………………….. bonds with each other.
Water is an important ………………………………….. in living organisms because
most biochemical reactions take place in aqueous solution. Water also has a high
………………………………….., which means that its temperature remains relatively
stable despite large changes in the temperature of the surrounding environment.
(Total 5 marks)
12. Read through the following account of compounds used for energy storage in cells, then write on the
dotted lines the most appropriate word or words to complete the account.
Water is the universal …………………………….. in living organisms. Molecules
which dissolve easily in water can produce osmotic effects. A high concentration of
small, soluble molecules within a cell can cause water to .......................…………..
the cell. This effect is reduced if the molecules used for storage in a cell
are …………………………….. . Therefore energy storage compounds are usually
either polysaccharides or …………………………….. . Examples of storage
polysaccharides include starch and …………………………….. Starch is found
mainly in …………………………….. cells.
(Total 6 marks)
13. A solution thought to contain either a reducing sugar or a non-reducing sugar was tested with Benedict’s
reagent.
(a) Describe how the presence of a reducing sugar is detected using Benedict’s reagent.
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(2)
(b) If the test was negative for reducing sugars, describe what steps you would need to carry out before you
could show that a non-reducing sugar was present.
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(3)
(c) Describe how Benedict’s reagent could be used to compare the concentrations of reducing sugar present
in two solutions.
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(3)
(Total 8 marks)
