Biochemistry Sow
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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 eek 1
2
Lesson title
Syllabus link
Amino Acids
(a) explain the term primary structure of proteins.
Protein Structure
(a) explain the term primary structure of proteins. (b) describe the secondary structure of proteins: α-helix and βpleated 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.
Suggested Activities
Homelearning
Introduction to amino acids, including zwitterions and the peptide bond. Use of models to build the structure of a protein. Use of photographs of proteins to show the folding that occurs. Questions relating to the bonding that occurs in the folding of a protein
Essay on the chemical importance of water.
Demo the protein in a egg 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. Practical, use of amylase on starch, protease on protein
Write up experiment
Design a fact sheet for a general studies class to explain the formation of a protein. You should include diagrams to illustrate the explanation and a glossary of the key scientific terms.
(d) describe the quaternary structure of proteins, for example: haemoglobin including the role of Fe2+.
3
Protein denaturation
(e) explain denaturation of proteins by heavy metal ions, extremes of temperature and pH changes (see also 5.6.2(d)).
4
What is an enzyme?
(a) describe the behaviour of enzymes as catalysts of high activity and specificity.
5
How do
(b) explain the relationship between enzyme and substrate concentrations of biochemical systems.
Lock and key and induced
Produce a list of twenty enzymes – name, substrate, product and where they are naturally found.
enzymes work?
(c) explain the concept of an active site in the structure of an enzyme.
6
Enzyme inhibition
(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.
7
Enzyme immobilisation
(e) explain the advantages of immobilising enzymes.
Carbohydrates Monosaccharid es and dissacharides
(a) describe the open-chain structure of a pentose (for example: ribose) and a hexose (for example: glucose).
Carbohydrates Polysaccharide s
(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, 1β4 and 1α-6 links).
8
9
(f) state the commercial and industrial uses of enzymes, typified by biological washing powders.
(b) describe the α- and β-pyranose ring structures of D-glucose.
fit
Model making to show how enzymes can be inhibited by competitive and non competitive chemicals. Immobilisation of lactase practical
Essay Immobilisation of enzymes and commercial uses
Use of molecular models to make the mono and dissacharides
Carbohydrate questions
Practical to look at the solubility of glucose versus starch. Use ideas about structure to explain the differences
Account to relating the structure of cellulose, starch and glycogen to their functions
Practical to make soap?
Revision for Interim exam
Write up practical
(c) describe the structure of a disaccharide including the nature of the glycosidic link, typified by maltose and cellobiose.
(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 membranes
(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.
Explanation of phospholipids making membranes.
(d) describe the structure and function of phosphoglycerides in the formation of bimolecular layers.
11
Lipids as an energy source
(e) explain that (i) lipids, treated simply as (CH2)n, are essentially a concentrated energy store of carbon and hydrogen;
Exam plus questions relating to enthalpy changes occurring when
Produce mark scheme for the exam.
(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.
glucose and fatty acids are burnt.
12
Building nucleic acids
(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.
Extracting DNA experiment.
Questions about lipids
13
DNA versus RNA
(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.
Similarities and differences between DNA and RNA
Questions about DNA
14
Transcription and Translation
(c) explain the role of DNA (i) in the replication of genetic information; (ii) in coding for m-RNA by transcription.
Marketplace lesson, students to work in three groups of three to learn and teach about transcription, translation and amino acid activation.
Revision for examination
(d) describe the role of m-RNA and t-RNA in coding for proteins by translation.
15
Exam Preparation
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 eek 1
2
Lesson title
Syllabus link
Amino Acids
(a) explain the term primary structure of proteins.
Protein Structure
(a) explain the term primary structure of proteins. (b) describe the secondary structure of proteins: α-helix and βpleated 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.
Suggested Activities
Homelearning
Introduction to amino acids, including zwitterions and the peptide bond. Use of models to build the structure of a protein. Use of photographs of proteins to show the folding that occurs. Questions relating to the bonding that occurs in the folding of a protein
Essay on the chemical importance of water.
Demo the protein in a egg 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. Practical, use of amylase on starch, protease on protein
Write up experiment
Design a fact sheet for a general studies class to explain the formation of a protein. You should include diagrams to illustrate the explanation and a glossary of the key scientific terms.
(d) describe the quaternary structure of proteins, for example: haemoglobin including the role of Fe2+.
3
Protein denaturation
(e) explain denaturation of proteins by heavy metal ions, extremes of temperature and pH changes (see also 5.6.2(d)).
4
What is an enzyme?
(a) describe the behaviour of enzymes as catalysts of high activity and specificity.
5
How do
(b) explain the relationship between enzyme and substrate concentrations of biochemical systems.
Lock and key and induced
Produce a list of twenty enzymes – name, substrate, product and where they are naturally found.
enzymes work?
(c) explain the concept of an active site in the structure of an enzyme.
6
Enzyme inhibition
(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.
7
Enzyme immobilisation
(e) explain the advantages of immobilising enzymes.
Carbohydrates Monosaccharid es and dissacharides
(a) describe the open-chain structure of a pentose (for example: ribose) and a hexose (for example: glucose).
Carbohydrates Polysaccharide s
(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, 1β4 and 1α-6 links).
8
9
(f) state the commercial and industrial uses of enzymes, typified by biological washing powders.
(b) describe the α- and β-pyranose ring structures of D-glucose.
fit
Model making to show how enzymes can be inhibited by competitive and non competitive chemicals. Immobilisation of lactase practical
Essay Immobilisation of enzymes and commercial uses
Use of molecular models to make the mono and dissacharides
Carbohydrate questions
Practical to look at the solubility of glucose versus starch. Use ideas about structure to explain the differences
Account to relating the structure of cellulose, starch and glycogen to their functions
Practical to make soap?
Revision for Interim exam
Write up practical
(c) describe the structure of a disaccharide including the nature of the glycosidic link, typified by maltose and cellobiose.
(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 membranes
(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.
Explanation of phospholipids making membranes.
(d) describe the structure and function of phosphoglycerides in the formation of bimolecular layers.
11
Lipids as an energy source
(e) explain that (i) lipids, treated simply as (CH2)n, are essentially a concentrated energy store of carbon and hydrogen;
Exam plus questions relating to enthalpy changes occurring when
Produce mark scheme for the exam.
(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.
glucose and fatty acids are burnt.
12
Building nucleic acids
(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.
Extracting DNA experiment.
Questions about lipids
13
DNA versus RNA
(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.
Similarities and differences between DNA and RNA
Questions about DNA
14
Transcription and Translation
(c) explain the role of DNA (i) in the replication of genetic information; (ii) in coding for m-RNA by transcription.
Marketplace lesson, students to work in three groups of three to learn and teach about transcription, translation and amino acid activation.
Revision for examination
(d) describe the role of m-RNA and t-RNA in coding for proteins by translation.
15
Exam Preparation
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