Download Year 13 Winter Revision Guide

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.
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As Moving Image
The Year 13 MIA class are to revise all the content we have covered from
September, in particular film language terminology.
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As Psychology:
Social Influence, Memory & Attachment
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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
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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.
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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.
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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.
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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.