Chemistry A2

Marlborough School

Scheme of Work
 Biochemistry

Autumn Term – Marlborough School

Syllabus Content
5.6.1 Proteins

Content

• Review of appropriate material from A2 Chemistry – Module 2814 Chains,

Rings and Spectroscopy, 5.4.4(e)–(h).
• Amino acids, polypeptides and proteins.
• Protein structure: primary, secondary, tertiary and quaternary structures.
• Denaturation of proteins.

Assessment Outcomes
Candidates should be able to:

(a) explain the term primary structure of proteins.

(b) describe the secondary structure of proteins: α-helix and β-pleated sheet;
the stabilisation of these structures by hydrogen bonding.

(c) state the importance of the tertiary protein structure and explain its
stabilisation by R groups in the amino acid residues, in terms of ionic
linkages, disulphide bridges, hydrogen bonds and van der Waals’ forces.

(d) describe the quaternary structure of proteins, for example: haemoglobin

including the role of Fe2+.

(e) explain denaturation of proteins by heavy metal ions, extremes of

temperature and pH changes (see also 5.6.2(d)).
5.6.2 Enzymes

Content

• Enzymes: relationship between enzymes and substrates; active sites.

• Competitive and non-competitive inhibition.
• Industrial uses of enzymes.

Assessment Outcomes
Candidates should be able to:

(a) describe the behaviour of enzymes as catalysts of high activity and

specificity.

(b) explain the relationship between enzyme and substrate concentrations of

biochemical systems.

(c) explain the concept of an active site in the structure of an enzyme.

(d) distinguish between inhibition of enzymes:

(i) competitive inhibition by a similar substrate molecule competing for
the active site;
(ii) non-competitive inhibition by heavy metal ions.

(e) explain the advantages of immobilising enzymes.

(f) state the commercial and industrial uses of enzymes, typified by biological
washing powders.

5.6.3 Carbohydrates

Content

• Monosaccharides.
• Disaccharides.
• Polysaccharides.

Assessment Outcomes
Candidates should be able to:

(a) describe the open-chain structure of a pentose (for example: ribose) and a
hexose (for example: glucose).

(b) describe the α- and β-pyranose ring structures of D-glucose.

(c) describe the structure of a disaccharide including the nature of the

glycosidic link, typified by maltose and cellobiose.
(d) describe the structure of polysaccharides, for example: cellulose and
starch (amylose and amylopectin):
(i) as condensation polymers;
(ii) in terms of their glycosidic links (to include 1α-4, 1β-4 and 1α-6
links).

(e) describe the enzyme and acid hydrolysis of the glycosidic linkage.

(f) compare the solubilities of monosaccharides and polysaccharides in water,

in terms of hydrogen bonding.

(g) suggest how the structures and properties of cellulose, starch and
glycogen make them suitable for their role as structural or storage polymers
in plants and animals.

5.6.4 Lipids and membrane structure

Content

• Biological functions of lipids.

• Triglycerides.
• Phosphoglycerides; formation of bilayers.

Assessment Outcomes
Candidates should be able to:

(a) describe the structure and function of triglyceryl esters.

(b) describe the hydrolysis of triglycerides as a source of fatty acids, for

example: in soapmaking.

(c) explain the solubility of triglycerides in non-polar solvents.

(d) describe the structure and function of phosphoglycerides in the formation

of bimolecular layers.

(e) explain that

(i) lipids, treated simply as (CH2)n, are essentially a concentrated
energy store of carbon and hydrogen;
(ii) carbohydrates, treated simply as (CH2O)n, are made up of partly
oxidised carbon and hydrogen units allowing more 'instant access' to
energy;
(iii) why, on complete oxidation, lipids release more energy per
gramme than carbohydrates.

Treatment of metabolic stages is not required.

5.6.5 Nucleic acids

Content

• Nucleotides and nucleic acids.

• DNA and RNA; base pairing.
• DNA and genetic information.
• m-RNA and protein synthesis.

Assessment Outcomes
Candidates should be able to:

(a) describe, in simple terms, the structure of

(i) nucleotides;
(ii) the nucleic acids DNA and RNA (as condensation polymers of
nucleotides), including base pairing and the part played by hydrogen
bonding.

(b) describe the chemical and physical differences between DNA and RNA
molecules including
(i) their base pairs and sugars;
(ii) the double helix in DNA and single strand in RNA;
(iii) their molecular sizes.

(c) explain the role of DNA

(i) in the replication of genetic information;
(ii) in coding for m-RNA by transcription.

(d) describe the role of m-RNA and t-RNA in coding for proteins by translation.
 Biochemistry

Autumn Term - Marlborough School - Lesson Overview

W Lesson title Syllabus link Suggested Activities Homelearning
eek
1 Amino Acids (a) explain the term primary structure of proteins. Introduction to amino Essay on the chemical
acids, including importance of water.
zwitterions and the
peptide bond.
2 Protein (a) explain the term primary structure of proteins. Use of models to build the Design a fact sheet for a
Structure structure of a protein. general studies class to
(b) describe the secondary structure of proteins: α-helix and β-
pleated sheet; the stabilisation of these structures by hydrogen Use of photographs of explain the formation of a
bonding. proteins to show the protein. You should
folding that occurs. include diagrams to
(c) state the importance of the tertiary protein structure and
Questions relating to the illustrate the explanation
explain its stabilisation by R groups in the amino acid residues,
in terms of ionic linkages, disulphide bridges, hydrogen bonds bonding that occurs in the and a glossary of the key
and van der Waals’ forces. folding of a protein scientific terms.
(d) describe the quaternary structure of proteins, for example:
haemoglobin including the role of Fe2+.

3 Protein (e) explain denaturation of proteins by heavy metal ions, Demo the protein in a egg Write up experiment
denaturation extremes of temperature and pH changes (see also 5.6.2(d)).
and in meat being
denatured by heat, acid
and alkali. Use bacon and
egg to show this.
Use ideas about chemical
environments and kinetic
theory to explain this.
Practical – catalase, H202
and liver at various
temperatures to see if the
initial rate is affected or
effect of Cu2+ions.
4 What is an (a) describe the behaviour of enzymes as catalysts of high Practical, use of amylase Produce a list of twenty
activity and specificity.
enzyme? on starch, protease on enzymes – name,
protein substrate, product and
where they are naturally
found.
5 How do (b) explain the relationship between enzyme and substrate Lock and key and induced
concentrations of biochemical systems.
 enzymes work? fit
(c) explain the concept of an active site in the structure of an
enzyme.

6 Enzyme (d) distinguish between inhibition of enzymes: Model making to show Essay Immobilisation of
(i) competitive inhibition by a similar substrate
inhibition how enzymes can be enzymes and commercial
molecule competing for the active site;
(ii) non-competitive inhibition by heavy metal ions. inhibited by competitive uses
and non competitive
chemicals.
7 Enzyme (e) explain the advantages of immobilising enzymes. Immobilisation of lactase Write up practical
immobilisation practical
(f) state the commercial and industrial uses of enzymes, typified
by biological washing powders.

8 Carbohydrates (a) describe the open-chain structure of a pentose (for example: Use of molecular models Carbohydrate questions
ribose) and a hexose (for example: glucose).
- to make the mono and
Monosaccharid (b) describe the α- and β-pyranose ring structures of D-glucose. dissacharides
es and
dissacharides (c) describe the structure of a disaccharide including the nature
of the glycosidic link, typified by maltose and cellobiose.

9 Carbohydrates (d) describe the structure of polysaccharides, for example: Practical to look at the Account to relating the
cellulose and starch (amylose and amylopectin):
- solubility of glucose structure of cellulose,
(i) as condensation polymers;
Polysaccharide (ii) in terms of their glycosidic links (to include 1α-4, 1β- versus starch. Use ideas starch and glycogen to
s 4 and 1α-6 links). about structure to explain their functions
the differences
(e) describe the enzyme and acid hydrolysis of the glycosidic
linkage.

(f) compare the solubilities of monosaccharides and

polysaccharides in water, in terms of hydrogen bonding.

(g) suggest how the structures and properties of cellulose,

starch and glycogen make them suitable for their role as
structural or storage polymers in plants and animals.

10 Lipids and (a) describe the structure and function of triglyceryl esters. Practical to make soap? Revision for Interim exam
membranes
(b) describe the hydrolysis of triglycerides as a source of fatty
acids, for example: in soapmaking. Explanation of
phospholipids making
(c) explain the solubility of triglycerides in non-polar solvents. membranes.
(d) describe the structure and function of phosphoglycerides in
the formation of bimolecular layers.

11 Lipids as an (e) explain that Exam plus questions Produce mark scheme for
(i) lipids, treated simply as (CH2)n, are essentially a
energy source relating to enthalpy the exam.
concentrated energy store of carbon and hydrogen;
changes occurring when
 (ii) carbohydrates, treated simply as (CH2O)n, are glucose and fatty acids
made up of partly oxidised carbon and hydrogen units
are burnt.
allowing more 'instant access' to energy;
(iii) why, on complete oxidation, lipids release more
energy per gramme than carbohydrates.

12 Building nucleic (a) describe, in simple terms, the structure of Extracting DNA Questions about lipids
(i) nucleotides;
acids experiment.
(ii) the nucleic acids DNA and RNA (as condensation
polymers of nucleotides), including base pairing and
the part played by hydrogen bonding.

13 DNA versus (b) describe the chemical and physical differences between DNA Similarities and Questions about DNA
and RNA molecules including
RNA differences between DNA
(i) their base pairs and sugars;
(ii) the double helix in DNA and single strand in RNA; and RNA
(iii) their molecular sizes.

14 Transcription (c) explain the role of DNA Marketplace lesson, Revision for examination
(i) in the replication of genetic information;
and Translation students to work in three
(ii) in coding for m-RNA by transcription.
groups of three to learn
(d) describe the role of m-RNA and t-RNA in coding for proteins and teach about
by translation. transcription, translation
and amino acid
activation.
15 Exam
Preparation