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3.1.2 Carbohydrates
Identify the common monosaccharides glucose, galactose and fructose.
Describe the monosaccharides from which the disaccharides lactose, maltose and sucrose are made.
Explain what is meant by a glycosidic bond and how they form through condensation.
Describe how polymerisation of α-glucose can form starch or glycogen.
Describe how to carry out the: Benedict’s test for reducing/non-reducing sugars and iodine test for starch and explain what
Recall the structure of α -glucose and β –glucose and represent diagrammatically.
Explain why glycosidic bonds between α –glucose form starch or glycogen and how this relates to their function and proper
Explain why glycosidic bonds between β –glucose form cellulose and how this relates to its function and properties.
3.1.3 Lipids
Explain what a lipid is and describe the structure of triglycerides.
Explain how triglycerides form from fatty acids and glycerol and recall what an ester bond is.
Describe what an R group is and recognise, from diagrams, saturated and unsaturated fatty acids.
Describe the structure of phospholipids.
Explain the properties of phospholipids related to their structure.
Describe the different properties of triglycerides and phospholipids and compare the them .
Describe the stages of the and interpret the results of the emulsion test for lipids.
3.1.4 Proteins
Recall and describe the general structure of an amino acid.
Explain how dipeptides polypeptides form polypeptides through condensation of amino acids.
Explain the relationship between primary, secondary, tertiary and quaternary structure, and protein function
Explain the role of hydrogen bonds, ionic bonds and disulfide bridges in the structure of proteins.
Describe the Biuret test and how it can be interpreted.
Explain the variety of functions that proteins have and why they are so important to the body.
Describe how to separate biological compounds using thin layer/paper chromatography and interpret chromatograms and
Describe enzymes as catalysts that lower the activation energy and interpret energy level diagrams to identify the activatio
Explain and describe the lock and key theory and the induced fit model of enzyme action.
Evaluate the strengths of the induced fit model against the lock and key theory.
Use knowledge of tertiary structure to explain enzyme specificity and the formation of enzyme-substrate complexes.
Explain how temperature, pH, substrate concentration, enzyme concentration, and the presence of inhibitors affect enzym
Describe and explain trends within graphs, relating this to the tertiary structure of active sites and the effect of different va
Calculate rate of reaction from graphs and raw data, and explain the advantage of using initial rate.
Interpret graphs of enzyme catalysed reactions and apply knowledge to explain them.
In required practical 1: investigation into the effect of a named variable on the rate of an enzyme-controlled reaction.
3.1.6 ATP
Recall and describe the structure of ATP.
Explain how the hydrolysis of ATP to ADP and Pi is catalysed by the enzyme ATP hydrolase, and can be used to phosphoryla
Explain how ATP is resynthesized from ADP and Pi by the enzyme ATP synthase, during photosynthesis or respiration.
3.1.7 Water
Recall and describe the properties that are important in water: - as a metabolite, solvent, has a high heat capacity, has a lar
Describe and explain the properties of water linked to the polar nature of the molecule.
Explain the significance of these properties to living organisms and processes.
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3.3 Organisms exchange substances with their environment
Use these checklists to check your learning and revision. Enter Y - Secure knowledge N
3.3.1 Surface area to volume ratio
Explain relationship between the size or structure of an organism and its surface area to volume ratio.
Explain how changes to body shape and the development of systems as adaptations that facilitate exchange as this ratio reduc
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