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YEAR 13 DEC EXAMINATIONS 2016 REVISION PLANNER Name _______________________ Class ______ Tips For Staying Healthy During Exams 1. Eat regular meals (including breakfast) Eat wholegrain carbohydrates rather than sugary foods to maintain stable blood sugar levels. Sugary foods give an initial energy boost but this is not maintained and can lead to low energy and mood. Wholegrain carbohydrates include porridge oats, wholemeal bread, pasta and rice, potatoes, beans and pulses. 2. Eat healthy snacks Avoid junk food as it will reduce concentration and memory recall and will increase stress levels. Good healthy options are fresh, dried fruit, nuts, seeds, cottage cheese on celery sticks, cheese and oat or rice cakes, toast, popcorn, yoghurt and raw vegetables. 3. Eat foods rich in Omega 3 Omega 3 improves brain function and increases concentration. It also helps to improve your immune system when your body and mind are stressed. The best source of Omega 3 is oily fish such as mackerel, sardines, salmon, trout, and herring. 4. Keep well hydrated Dehydration can make it difficult to concentrate and causes tiredness and irritability. It is recommended we drink 6-8 glasses of water each day. Avoid sugary, caffeinated drinks as they will cause dehydration and a drop in energy levels after an initial boost. 5. Eating before the exam Try to have a light meal before each exam to supply your brain with enough fuel for maximum efficiency and therefore the greatest chance of success. 6. Don’t use electronic devices before bedtime Phones and tablets emit light that delays the release of the ‘sleep hormone’ melatonin. Without melatonin you will have poor quality sleep and therefore poor memory recall and concentration levels. Aim to get 8 hours sleep each night and avoid naps during the day. 7. Take regular exercise Regular exercise improves cognitive function, helping us process information more effectively. 8. If you're feeling really worried or anxious, ask for help. As English Literature Year 13 Revision list for Mrs McDonald: ‘The Handmaid’s Tale.” Features of dystopian fiction, Historical and social context , Secondary material – relevant quotations from critics on the dystopian features of the novel. Year 13 Revision list for Mrs Hyndman ‘A Doll’s House’ including key themes, characters, ideas, symbols Christina Rossetti poetry including key themes, devices, ideas, symbols For both: historical and social context; literary/artistic movements (e.g. wellmade play, melodrama, Pre-Raphaelites); the play in performance (lead actors, interpretations, responses from audiences and critics); relevant quotations from critics; areas of comparison or contrast between the texts, particularly in regard to main themes. ____________________________________________________________________ As Moving Image The Year 13 MIA class are to revise all the content we have covered from September, in particular film language terminology. ___________________________________________________________________ As Psychology: Social Influence, Memory & Attachment _________________________________________________________________________ Topics to Revise include As & A2 History The German Revolution 1918-19 The Weimar Constitution The Treaty of Versailles Political threats to Weimar Democracy 1923 The year of crisis Recovery and stability 1924-9 The Rise of the Nazis 1919-29 The Collapse of the Weimar Republic and The Rise of the Nazis The Nazis breakthrough to Power 1929-33 The Consolidation of Power January-March 1933 __________________________________________________________________________ Islam (Mrs Coleman) As Religion „ The life and work of Muhammad in its historical, religious and social context; his significance for Muslims - Social & Historical Background in the context of the Life of Muhammad - Religious Background in the context of the Life of Muhammad - Influence of these contexts on his life Year13 – (Miss McAlinden) Luke Understanding of the Gospel of Luke: Influence and role of the Pharisees and Sadducees in Luke’s Gospel. Possibly dating of Luke’s Gospel – Early, Intermediate and late date. Authorship – Internal and External evidence Purpose of Luke’s Gospel. ________________________________________________________________ As Maths Year 13 will do 2 Maths exams- C1 (Mrs Cumiskey’s paper) & M1 (Mr O’Boyle’s paper) C1 1. Algebra and Functions 2. Coordinate geometry in the (x,y) plane 3. Sequences and series 4 Differentiation 5 Integration M1 - Revision - Kinematics of a practical moving in a straight line with constant acceleration - Model an object moving vertically in a straight line under gravity - Speed time graphs/ Distance time graphs/ acceleration time graphs - Dynamics of particle moving in a straight line - F=ma - Solve problems involving forces by drawing diagrams and resolving - Resolve forces at an angle to the component that acts in a certain direction - Calculate magnitude of friction force using the coefficient. - Solve problems about particles on inclined planes by resolving forces parallel and perpendicular to the plane. __________________________________________________________________________ As Biology AS CCEA Biology Revision List December 2016 Molecules Students should be able to: Understand the importance of water as a solvent. Outline the role of inorganic ions – potassium, calcium, magnesium, iron, hydrogen carbonate, nitrate and phosphate: as components of biologically important compounds (calcium pectate, chlorophyll, haemoglobin, ATP, nucleic acids, phospholipids); in osmotic and buffering systems Recognise the occurrence, structure and function of carbohydrates: monosaccharides (α- and β- glucose, fructose, C6H12O6); condensation reactions in the synthesis of and hydrolysis reactions in the breakdown of disaccharides and polysaccharides; the glycosidic bond; maltose and sucrose as disaccharides; cellulose – a structural polymer of β-glucose; starch and glycogen as storage polymers of α-glucose; pentoses as components of nucleic acids (ribose and deoxyribose) and ATP (ribose). Recognise the occurrence, structure and function of lipids: lipids as fats and oils; triglycerides as condensation products of glycerol and fatty acids and the release of these on hydrolysis; saturated and unsaturated fatty acids; the structure and properties of phospholipids as components of membranes. Recognise the occurrence, structure and function of proteins: the general structure of an amino acid molecule; proteins as condensation products of amino acids and the release of these on hydrolysis; primary structure: the amino acid sequence of a polypeptide involving peptide bonds; secondary structure: α- helix and β- pleated sheet involving H-bonds; tertiary structure: the folding of a polypeptide involving; H-, ionic and disulphide bonds, hydrophobic interactions; quaternary structure: more than one polypeptide making up a protein; overall shape in relation to function in fibrous (collagen) and globular (enzyme) proteins; conjugated proteins (glycoprotein and haemoglobin) containing prosthetic groups; prions as a disease-causing protein, due to changes in secondary structure giving a form rich in β-sheets: - infection can occur through eating prion rich food; - prion diseases are neurodegenerative disorders such as scrapie, BSE in animals and CJD in humans. The occurrence, structure and function of nucleic acids: Nucleic acids as condensation products of nucleotides and the release of these on hydrolysis; Nucleotides as condensation products of a pentose sugar, a nitrogenous base and inorganic phosphate; Helical structure of DNA in terms of two antiparallel chains with specific base pairings; Comparison of DNA and RNA. The replication of DNA: Replication as a semi-conservative process involving opening the helix (by DNA helicase) followed by the synthesis of complementary nucleic acid chains alongside each of the existing chains to form two identical helices; The role of DNA polymerase; The Meselson-Stahl experiment. Describe biochemical tests to detect the presence of carbohydrates and proteins: iodine test; Benedict’s test; Clinistix (glucose specific tests); Biuret test; paper chromatography of amino acids: preparation, running and development of the chromatogram; calculation of Rf values. Enzymes Understand the structure of enzymes: enzymes as globular proteins and the concept of the active site and specificity; the role of cofactors and coenzymes. Understand the relationship between enzyme structure and function: catalysts that lower the activation energy through the formation of enzyme – substrate complexes; the Lock and Key hypothesis and Induced-fit hypothesis; effect of temperature, pH, substrate and enzyme concentrations on activity; enzyme inhibitors (competitive and non-competitive) Enzymes as biomarkers of disease: Some enzymes are only present or active during disease processes (e.g. white blood cells can release elastase during respiratory infections, hydrolysing the structural protein elastin within the lung leading to reduced lung function); That detecting the presence of these enzymes in clinical samples such as blood, urine and sputum can be used for diagnosis or monitoring the disease. Inhibitors as therapeutic drugs, including the use of enzymes that contribute to disease processes, which can be targeted with active site-directed inhibitors. Understand the application of immobilised enzymes in biotechnology: methods of immobilisation (physically or chemically securing enzymes on or inside an insoluble support material such as fibres, gels or plastic beads); immobilisation as a technique enabling cost-effective enzyme applications (increased enzyme stability, facilitation of continuous flow processes, enzymefree product though with reduced activity due to inaccessibility of some active sites); diagnostic reagent strips as biosensors (e.g. clinistix) or inhibitors as biosensors. Describe experimental investigation of factors affecting enzyme activity: effect of temperature, pH, substrate and enzyme concentrations on enzyme activity; illustration of enzyme immobilisation; use of a colorimeter to follow the course of a starch – amylase catalysed reaction. Viruses Students should be able to: Understand the structure of bacteriophages (phages) and the human immunodeficiency virus (HIV): phages containing DNA bounded by a protein coat; HIV containing RNA bounded by a protein coat and a lipid bilayer containing glycoprotein; and, as a retrovirus, containing reverse transcriptase whereby RNA is used to synthesise viral DNA. Appreciate that viruses replicate in host cells (thereby destroying them): phages invade bacteria in which they replicate, destroying the bacterial cells; HIV invades a type of lymphocyte (helper T-cell) thereby weakening the immune system Cells Students should be able to: Describe the ultrastructure of eukaryotic and prokaryotic cells: prokaryotic cells (e.g. bacteria) as those without nuclei, mitochondria or endoplasmic reticulum and possessing naked, circular DNA, small ribosomes, possibly plasmids, and a cell wall; eukaryotic cells as those with a membrane-bound nucleus, chromosomes (helical DNA with a histone protein coat), mitochondria, endoplasmic reticulum, ribosomes, Golgi apparatus, vesicles, lysosomes, microtubules. Understand the structure and function of membranes: membrane structure (fluid mosaic model): phospholipid bilayer, intrinsic and extrinsic protein, carbohydrate glycocalyx, glycoproteins and glycolipids, cholesterol (in animal cells); functions of membrane components: proteins/glycoproteins as carriers, hydrophilic channels, enzymes, receptors, antigens, recognition features; cholesterol in membrane stability. Understand the structure and function of eukaryotic cell components: membranes (fluid mosaic model) as structures surrounding cells and contributing to their internal structures; mitochondria (envelope, cristae and matrix); chloroplasts (envelope, lamellae, thylakoids, grana, stroma, lipid droplets and starch grains); rough endoplasmic reticulum (a membrane system with attached ribosomes); ribosomes as sites of protein synthesis; smooth endoplasmic reticulum; golgi apparatus; lysosomes; microtubules (centrioles and cell spindle); plasmodesmata as plant cell to cell junctions; nuclear components: Chromosomes (DNA and histones as constituents; euchromatin and heterochromatin; nucleolus (the location of the DNA which codes for ribosomal RNA); the nuclear envelope as a perforated double membrane; the outer membrane of the envelope is encrusted with ribosomes and is the site of origin of RER. Compare eukaryotic cell structure: plant cells as protoplasts bordered by an extracellular cellulose cell wall and possessing chloroplasts and vacuole(s); neighbouring cell walls adhered by a middle lamella (a sticky material composed of calcium pectate); fungal cells as protoplasm (often multinucleate) bounded by an extracellular wall of chitin; animal cells as lacking chloroplasts and a cell wall and possessing centrioles. Understand the use of microscopy in examining cell structure: light microscope; electron microscope (TEM/SEM). Examine photomicrographs and electron micrographs (TEM/SEM): Recognise cell structures from photomicrographs and electron micrographs (TEM/SEM); Calculation of true size (in μm) and magnification, including the use of scale bars. __________________________________________________________________________ AS Chemistry Revision list Formulae and equations: writing and balancing equations Amounts of Substance: Mole, Avogadro’s Number, molar mass, Reacting Masses of substances Water of crystallisation, anhydrous, hydrated etc. Atomic Structure: Protons, electrons, neutrons, Atomic number, Atomic mass, Relative Atomic Mass determination and calculation of, Relative molecular mass etc. S,p,d notation of electronic configuration, evidence for shells-ionisation energies etc. Atomic spectroscopy- calculations associated with this using E=hf and v= freq. x wavelength etc. Convergence limit. Bonding and structure: ionic, covalent and coordinate bonding- dot and cross diagrams (outer Electrons only), polarity of bonds, electronegativity, dipoles etc. Shapes of molecules and ions: VSEPR Theory- repulsion of electron pairs in molecular shapes. Intermolecular forces: Van der Waals forces, dipole forces, H-bonding. Unit AS 2: Human Body Systems The Respiratory System Demonstrate an understanding of the chemical composition of haemoglobin in relation to its role in oxygen transport. Demonstrate an understanding of the concept of partial pressure of oxygen and its effect on oxygen transport by haemoglobin. Demonstrate an understanding of the Bohr effect on oxygen transport by haemoglobin and the physiological advantage of this for a tissue. Demonstrate an understanding of the structure and functioning of the components of the respiratory system, how these function individually and how the respiratory system functions as a whole. Demonstrate an understanding of the factors affecting the rate of gas exchange. Demonstrate an understanding of gas exchange in a mammal. Explain methods for monitoring the respiratory system. Homeostasis Describe the concept of homeostasis and the components of homeostatic mechanism. Describe the role of hormones in body function. Describe the monitoring of glucose levels. Explain how blood is buffered to maintain normal blood pH range (7.35-7.45) and how blood pH is monitored. Describe the causes and consequences of blood becoming acidic or alkaline. Describe the monitoring of oxygen saturation (SaO2%; normal levels 95-99%) by pulse oximeter and conditions which may lead to reduced SaO2% levels. AS3: Aspects of physical chemistry in industrial processes. Chemical calculations Use chemical formula and relative atomic masses to calculate the number of moles of its substance Use balanced equations to calculate required quantities of reactants, theoretical yields of products, percentage yield and theoretical yield. Describe the steps to making a standard solution Using titration results, calculate the concentration of an acid in mol/dm3 Enthalpy Demonstrate knowledge of enthalpy changes in combustion and neutralisation reactions. Become familiar with the terms; exothermic, endothermic, enthalpy of combustion and enthalpy of neutralisation. Define Hess’s law Construct enthalpy cycles for calculating enthalpy of combustion from enthalpy of formation and for calculating enthalpy of reaction from enthalpies of formation. Use average bond enthalpies to calculate the enthalpy change of a reaction (mean bond enthalpy questions) Kinetics Construct energy level diagrams Explain the factors that affect the rate of reaction, to include concentration, pressure, temperature and use of a catalyst. Use Maxwell-Boltzmann distribution curve to explain the effects of change in temperature and the action of a catalyst. Equilibrium Define the term reversible reaction Recall the conditions required in the Haber process Evaluate data to explain the need to reach a compromise between yield and rate of reaction for the Haber process.