Cumulative Flashcards
What is the structure of the cell-surface membrane?
The cell surface membrane is a phospholipid bilayer. Phospholipids have hydrophilic phosphate heads and hydrophobic fatty acid tails, so the heads point outwards and the tails point inwards. It also contains intrinsic and extrinsic proteins, glycolipids and glycoproteins on the exterior surface, and cholesterol molecules.
Explain the role of cholesterol in cell membranes.
Restricts movement of other molecules making up the membrane, increasing rigidity
Describe how movement across membranes occurs by simple diffusion
Lipid-soluble, non-polar or very small substances move from an area of higher concentration to an area of lower concentration down the concentration gradient across the phospholipid bilayer. This is a passive process, meaning it requires no energy from ATP.
Describe how movement across membranes occurs by facilitated diffusion
Water-soluble, polar, large molecules move down the concentration gradient through specific channel and carrier proteins. This is a passive process, meaning it requires no energy from ATP.
Explain the role of carrier and channel proteins in facilitated diffusion
Channel proteins have a hydrophilic pore filled with water which allows water-soluble molecules to diffuse across the membrane. Carrier proteins facilitate the diffusion of larger molecules. When complimentary substances bind to the binding site, the carrier protein will change shape via conformational change to transport the substance across the membrane.
Describe how movement across membranes occurs by osmosis
Water moves from an area of high water potential to an area of low water potential down a water potential gradient through a partially permeable membrane until equilibrium. This is a passive process, meaning it requires no energy from ATP.
What is the maximum water potential and what substance would have this amount?
0ψ or 0kPA, distilled water
Describe how movement across membranes occurs by active transport
Substances move from an area of lower concentration to an an area of high concentration, against the concentration gradient. This requires energy from the hydrolysis of ATP and also requires specific carrier proteins
Describe the role of carrier proteins and the importance of the hydrolysis of ATP in active transport
The complementary substance binds to specific carrier protein, and ATP also binds to the carrier protein, resulting in it being hydrolysed into ADP + Pi, releasing energy. This energy is used to change the shape of the carrier protein, transporting the substance to the other side of the membrane. Then, the inorganic Phosphate is released, causing the protein to return to the original shape
Describe how movement across membranes occurs by co-transport
Two different substances bind to a
co-transporter protein (type of carrier protein) and move through it simultaneously. Often this involves movement of one substance against its concentration gradient and the movement of the other down its concentration gradient
Name 4 factors affecting the rate of movement across cell membranes and explain how they affect it.
- Surface area of membrane: Increasing surface area increases the rate of movement
- Number of channel/carrier proteins: Increasing number of channel / carrier proteins increases rate of facilitated diffusion / active transport
- Concentration gradient: Increasing concentration gradient increases rate of facilitated diffusion (until number of channel / carrier proteins becomes a limiting factor as all are saturated), simple diffusion and osmosis.
- Water potential gradient: Increasing water potential gradient increases rate of osmosis
Explain the adaptations of some specialised cells in relation to the rate of transport across their membranes
- The membrane is folded, for example in microvilli in ileum. This increases surface area, increasing the rate of transport.
- More protein channels / carriers for facilitated diffusion or active transport (Carrier Proteins only)
- Large number of mitochondria to release more ATP and therefore releasing more energy by aerobic respiration for active transport
What is genetic diversity?
Number of different alleles of genes in a population
What are alleles and how do they arise?
Variations of a particular gene, they arise by mutation
What is a population?
A group of interbreeding individuals of the same species.
Explain the importance of genetic diversity
Enables natural selection to occur, as in certain environments, a new allele of a gene might be beneficial. Having advantageous genes increases chances of survival and reproductive success.
What is evolution and how does it occur?
Change in allele frequency over many generations in a population. It occurs through the process of natural selection
Explain the principles of natural selection in the evolution of populations
MARIA
* Mutation: Random gene mutations can result in new alleles of a gene
* Advantage: In certain environments, the new allele might benefit its possessor, so the organism has a selective advantage
* Reproductive success: Possessors are more likely to survive and have increased reproductive success
* Inheritance: Advantageous allele is inherited by members of the next generation (offspring)
* Allele frequency Over many generations, the advantageous allele increases in frequency in the population
Describe 3 types of adaptations
- Anatomical - structural / physical features that increase chance of survival
- Physiological - processes / chemical reactions that increase chance of survival
- Behavioural - ways in which an organism acts that increase chance of survival
What is directional selection?
Organisms with an extreme variation of a trait has a selective advantage over the other extreme. This results in an increased frequency of organisms with alleles for the extreme trait. An example is antibiotic resistance in bacteria.
What is stabilising selection?
Organisms with an average variation of a trait has a selective advantage. This results in an increased frequency of organisms with alleles for the average trait. An example is human birth weight.
What is disruptive selection?
Organisms with either extreme
variation of a trait has a selective advantage. This results in an increased frequency of organisms with alleles for both extremes of the trait. An example is bird beak size
Name 2 groups of Lipids
Triglycerides and Phospholipids
Describe the structure of a fatty acid.
Has a variable R Group which is a hydrocarbon chain which is either saturated or unsaturated. It also has a Carboxyl group.
What is the difference between saturated and unsaturated fatty acids?
Unsaturated fatty acids contain one or more Carbon-Carbon double bonds, creating kinks in the hydrocarbon chain. Saturated fatty acids contain no Carbon-Carbon double bonds, and therefore all Carbons are fully saturated with Hydrogen.
How do triglycerides form?
Triglycerides consist of 1 glycerol molecule and 3 fatty acids, which join via condensation reactions. Therefore, 3 molecules of water are released and 3 ester bonds form.
Explain how the properties of triglycerides are related to their structure.
The hydrolysis of the fatty acid chains releases a lot of energy, meaning that triglyceride molecules are ideal energy stores. Also, the fatty acid chains are hydrophobic, meaning that triglyceride molecules are insoluble in water. Therefore, the molecules do not affect water potential, so no osmotic action occurs, damaging cells.
Describe the difference between the structure of triglycerides and phospholipids.
One of the fatty acids of a triglyceride is substituted for a phosphate group in a phospholipid.
Describe how the properties of phospholipids relate to their structure.
The phosphate group is hydrophilic and the fatty acid chains are hydrophobic. Therefore they can form membranes as they are selectively permeable, allowing certain substances into the cell and not others.
Describe the test for lipids.
Add ethanol and shake, and then add water. If the test is positive, a milky emulsion will form on top.
What is independent measures design? Give a strength and a weakness
Each participant only takes part in one of the conditions.
+ Order effects will not affect the results
- Differences between conditions may be due to participant variables
What is repeated measures design? Give a strength and a weakness
Each participant takes place in all of the conditions
+ Participant variables will not affect the results
- Order effects may affect the results
How can order effects be reduced?
Counterbalancing
What is the matched pairs design? Give a strength and a weakness
Each participant takes part in one condition, however each participant is
matched according to certain characteristics with another participant in the
other condition.
+ The effect of order effects and participant variables are reduced
- Can be time consuming or difficult to match participants
What is a laboratory experiment? Give a strength and a weakness
A laboratory experiment is an experiment carried out in a highly controlled environment, such as a laboratory.
+ Researchers can control for extraneous variables and ensure the procedure is
fully standardised and replicable, increasing reliability
- Results may lack ecological validity, as the artificial environment may cause unnatural behaviour from the participants
What is a field experiment? Give a strength and a weakness
A field experiment is an experiment carried out the participants’ natural setting
+ Results are likely to be high in ecological validity as participants’ behaviour will be more natural
- Researchers have little control over extraneous variables, therefore decreasing reliability
What is a quasi experiment? Give a strength and a weakness
A quasi experiment is an experiment in which the IV is not directly manipulated by the researcher
+ Useful for conducting research into naturally occurring variables or variables that would be unethical or impractical to manipulate
- Low reliability as the researcher has no control over the IV
What is a monomer?
A smaller, repeating molecule from which larger polymers are made
What is a polymer?
A larger molecule which is made up of identical repeating monomers.
What is a condensation reaction?
A reaction in which two molecules join together, forming a covalent bond and releasing a molecule of water.
What is a hydrolysis reaction?
A reaction in which the covalent bond between two molecules is broken, which uses up a molecule of water.
Which polymer consists of repeating nucleotides?
Polynucleotides (DNA or RNA)
Which polymer consists of repeating monosaccharides?
Polysaccharides
Which polymer consists of repeating amino acids?
Polypeptides (Proteins)
What is the difference between alpha and beta glucose?
In α-glucose, the H is above the OH whereas in β-glucose, the OH is above the H
Draw a molecule of alpha glucose.
https://static.aqa.org.uk/assets/image/0018/235440/00055366-DA00046397-DB.png
Draw a molecule of beta glucose
https://static.aqa.org.uk/assets/image/0008/235439/00055366-DA00046396-DB.png
What are isomers?
Molecules with the same molecular formula but differently arranged atoms.
What are disaccharides and how are they formed?
A disaccharide is two monosaccharides joined together with a glycosidic bond. They are formed by a condensation reaction, which releases a molecule of water.
Which disaccharide does Glucose and Glucose make?
Maltose
Which monosaccharides make Maltose?
Glucose and Glucose
Which disaccharide does Glucose and Fructose make?
Sucrose
Which monosaccharides make Sucrose?
Glucose and Fructose
Which disaccharide does Glucose and Galactose make?
Lactose
Which monosaccharides make Lactose?
Glucose and Galactose
What are polysaccharides and how are they formed?
Polysaccharides are made up of many (more than 2) monosaccharides, joined together with glycosidic bonds. They are formed by many condensation reactions, releasing water molecules.
Describe the basic function and structure of starch.
Starch acts as an energy source in plant cells. It is a polysaccharide of alpha glucose. It contains both Amylose and Amylopectin. Amylose has 1-4 glycosidic bonds and is therefore unbranched. Amylopectin has both 1-4 and 1-6 glycosidic bonds, meaning that it is branched.
Describe the basic function and structure of glycogen.
Glycogen acts as an energy store in animal cells. It is a polysaccharide of alpha glucose. It has both 1-4 and 1-6 glycosidic bonds. Therefore, it is branched.
Describe the basic function and structure of cellulose.
Cellulose acts as structural support in plant cells. It is found in the cell walls of plant cells. It is a polysaccharide of beta glucose, held together by 1-4 glycosidic bonds forming straight unbranched chains. Chains are joined together with hydrogen bonds forming microfibrils.
Explain how the structure of starch is related to its function.
Starch is helical, so it is compact for storage in cell. Also, it is a large molecule, meaning it can not leave the cell. It is also insoluble in water, meaning that it does not affect the water potential of the cell, so no osmotic action which could damage the cell occurs. Also, it is branched to increase the surface area for faster hydrolysis.
Explain how the structure of glycogen is related to its function.
Glycogen is branched are is therefore compact and more molecules can fit in small area. Also, the branching results in a larger surface area for the enzymes to quickly hydrolyse the glycosidic bonds to release glucose. Also, it is a large molecule meaning it can not leave the cell. It is also insoluble in water, meaning that it does not affect the water potential of the cell, so no osmotic action which could damage the cell occurs
Explain how the structure of cellulose is related to its function.
Every second β-glucose molecule is inverted in a long, straight, unbranched chain. Many hydrogen bonds link parallel strands (crosslinks) to form microfibrils. Hydrogen bonds are strong in large quantities, so provides strength to plant cell walls
Describe the test for reducing sugars
Firstly, add Benedict’s solution, which is blue to the sample. Next, heat the sample in a water bath. A positive test will result in a green, yellow, orange or red precipitate depending upon on the concentration of reducing sugars.
Describe the test for non-reducing sugars.
If the result of the Benedict’s test is negative, there still could be non-reducing sugar present. Heat in a boiling water bath and add acid in order to hydrolyse into reducing sugars. Next, neutralise with alkali (e.g. sodium bicarbonate) Now, carry out the Benedicta test as normal by heating sample in a boiling water bath with Benedict’s solution. Positive result = green / yellow / orange / red precipitate.
What is the one example of a non reducing sugar (that’s on the specification)?
Sucrose
Suggest a method to measure the quantity of sugar in a solution without a colorimeter.
Carry out a Benedict’s test, then filter and dry the precipitate. Then, measure the mass of the precipitate.
Suggest a method to measure the quantity of sugar in a solution using a colorimeter.
First, make a dilution series of sugar solutions of known concentrations. Next, heat a set volume of each sample with a set volume of Benedict’s solution. Use a colorimeter to quantitively measure the absorbance of each known concentration, and plot a calibration curve with . concentration on the x axis and absorbance on the y axis, and draw a line of best fit. Repeat the Benedict’s test with the unknown sample and find the concentration on the graph which is associated with the absorbance of the unknown sample.
Describe the biochemical test for starch.
Add iodine dissolved in potassium iodide, which is orange/brown. A positive result will cause a colour change to blue/black
Draw the general structure of an amino acid.
https://cdn.sanity.io/images/p28bar15/green/e7a792fa03f686507301a1d00a82af36777d3f91-960x670.png
What is the molecular formula of the carboxyl group?
COOH
What is the molecular formula of the amine group?
NH₂
How many amino acids are common in all organisms and how do they vary?
There are 20 amino acids that are common in all organisms and they differ only in their R group side chain.
How do amino acids join together?
Amino Acids join together via a condensation reaction, removing a water molecule. A Peptide bond is formed between the carboxyl group of one amino acids and the amine group of the other.
What is a dipeptide?
2 amino acids joined together with peptide bonds.
What is a polypeptide?
More than 2 amino acids joined together with peptide bonds.
What is the primary structure of a protein?
Sequence of amino acids in a polypeptide chain, joined by peptide bonds.
What is the secondary structure of a protein?
The folding of the polypeptide chain into alpha helices or beta pleated sheets due to hydrogen bonding between amino acids (between NH group of one amino acid and C=O group of the other)
What is the tertiary structure of a protein?
The 3D folding of the polypeptide chain due to interactions between the R groups of the amino acids. Therefore, hydrogen bonds, ionic bonds and disulphide bridges are formed.
What is the quaternary structure of a protein?
Made up of more than one polypeptide chain, formed by interactions between polypeptides.
Describe the test for proteins.
Add Biuret reagent (sodium hydroxide + copper II sulphate), which is blue. A positive result will cause a colour change to lilac. This indicates the presence of peptide bonds and therefore the presence of proteins.
How do enzymes act as a biological catalyst?
Enzymes catalyse reaction by lowering the activation energy. This speeds up the rate of reaction as less energy is needed to start it.
Describe the lock and key model of enzyme action.
Substrate binds to the active site, which is completely complimentary to it. They bind to form an enzyme-substrate complex.
Describe the induced fit model of enzyme action.
The substrate binds to the active site, which is not completely complimentary. This causes the active site to change shape so that it becomes complimentary to the substrate and an enzyme-substrate complex forms. This causes bonds in the substrate to change, lowering activation energy.
How have models of enzyme action changed over time?
Initially, the accepted model of enzyme action was the lock and key model, which stated that the active site is fixed and it is exactly complimentary to the substrate. New molecular evidence has suggested the induced fit model, which states that the active site changes shape slightly in order for the substrate to be able to fit.
Explain the specificity of enzymes.
The specific tertiary structure determines the shape of the active site. This is dependent on the sequence of amino acids (primary structure). The active site is complimentary to a specific substrate, and only this substrate can bind to the active site. The active site slightly changes shape in order for the substrate to fit, forming an enzyme-substrate complex.
Describe and explain the effect of enzyme concentration on the rate of enzyme-controlled reactions.
As enzyme concentration increases, the rate of reaction also increases. The rate increases because the concentration of enzymes is increasing, and there are more available active sites for substrate molecules to bind to, and therefore more enzyme-substrate complexes are formed. At this point, enzyme concentration is the limiting factor as there is excess substrate. At a certain point, the substrate concentration becomes the limiting factor, so the rate will stop increasing because all of the substrates will be in use.
Describe and explain the effect of substrate concentration on the rate of enzyme-controlled reactions.
As substrate concentration increases, the rate of reaction also increases. The rate increases because the concentration of substrates is increasing, and there are more substrate molecules that can bind to active sites, and therefore more enzyme-substrate complexes are formed. At this point, substrate concentration is the limiting factor as there is an excess of enzyme active sites, but at a certain point, the enzyme concentration becomes the limiting factor, so the rate will stop increasing because all of the enzymes will be saturated.
Describe and explain the effect of temperature on the rate of enzyme-controlled reactions.
As temperature increases up to the optimum, the rate of reaction increases because the molecules have more kinetic energy, meaning that more collisions between enzymes and substrate molecules will occur, leading to more enzyme-substrate complexes being formed. After the optimum, the rate of reaction decreases as the enzymes denature. Due to the high temperatures, the hydrogen bonds and ionic bonds in the tertiary structure of the enzyme break, changing the shape of the active site. Therefore, the active site is no longer complimentary, meaning that fewer enzyme-substrate complexes can form.
Describe and explain the effect of pH on the rate of enzyme-controlled reactions.
If the pH decreases or increases too much beyond the optimum, the rate of reaction decreases. This is because the H+ and OH- ions interfere with the hydrogen bonds and ionic bonds in the tertiary structure of the enzyme. Therefore, the shape of the active site changes and is no longer complimentary to the substrate, meaning that fewer enzyme-substrate complexes can form.
Describe and explain the effect of competitive inhibitors on the rate of enzyme-controlled reactions.
As the concentration of competitive inhibitors increases, the rate of reaction decreases. Competitive inhibitors have a similar shape to the substrate, and they therefore compete for the active site. This means that the active site is occupied, so the substrate can’t bind to the active site and fewer enzyme-substrate complexes can form. Increasing the concentration of substrate will reduce the effect of the competitive inhibitor as the substrate will begin to outcompete the inhibitor.
Describe and explain the effect of non-competitive inhibitors on the rate of enzyme-controlled reactions.
As the concentration of non-competitive inhibitor increases, the rate of reaction increases. Non-competitive inhibitors bind to the allosteric site, away from the active site. This leads to the tertiary structure of the enzyme changing, and the shape of the active site changing. Therefore, the active site is no longer complimentary to the substrate, so the substrate can not bind and fewer enzyme-substrate complexes form. Increasing substrate concentration will have no effect on the rate of reaction as the change to the tertiary structure is permanent.
Draw and label the general structure of a nucleotide.
https://images.squarespace-cdn.com/content/v1/5c5aed8434c4e20e953d6011/1600528627495-YZ3SZ4AQ5LOSINZEEX1I/nucleotide.jpg
Name 5 variables that could affect the rate of enzyme-controlled reaction.
Enzyme concentration, Substrate concentration, Temperature, pH, Inhibitor concentration.
What is the basic function of RNA in living cells?
Transfers genetic information from DNA to ribosomes.
What does a ribosome consist of?
RNA and Proteins
What is the basic function of DNA in living cells?
Carries genetic information, which codes for proteins.
Describe 3 differences between DNA and RNA.
In a DNA nucleotide, the pentose sugar in deoxyribose, whereas in RNA it is ribose. DNA contains the nitrogenous bases A, T, G and C, whereas RNA contains A, U, G and C. DNA molecules are double stranded and much larger than RNA molecules, which are much smaller and usually single stranded.
How do nucleotides join together to form polynucleotides?
Nucleotides join via condensation reactions, which remove water molecules. This forms phosphodiester bonds between the phosphate group of one nucleotide and the deoxyribose/ribose of the other.
Why did many scientists originally doubt that DNA carried the genetic code?
DNA is a chemically simplistic molecule which consists of very few components. Many scientists believed that the molecule that carries the genetic code would be much more complex.
Describe the structure of DNA.
DNA is a polynucleotide. Each nucleotide is formed from a deoxyribose pentose sugar, a phosphate group, and a nitrogenous base. Adjacent nucleotides are joined by phosphodiester bonds, and the 2 polynucleotide chains are joined by hydrogen bonds between complimentary base pairs (Adenine and Thymine, Guanine and Cytosine) This forms a double helix structure.
Describe the structure of RNA.
RNA is Polynucleotide. Each nucleotide is formed from a ribose pentose sugar, a phosphate group and a nitrogenous base (Adenine, Uracil, Guanine or Cytosine). Phosphodiester bonds join adjacent nucleotides, forming a single helix.
How does the structure of DNA relate to it’s function?
- Double stranded - Both can act as template strands for semi-conservative replication.
- Hydrogen bonds between complimentary base pairs are weak - strands can be easily separated for replication.
- Complimentary base pairing - Accurate replication
- Many hydrogen bonds between complimentary base pairs - strong, stable molecule
- Double helix with sugar phosphate back bone - protects the bases and hydrogen bonds
- Long molecule - can store lots of genetic information, which codes for proteins.
- Coiled double helix - compact for storage
How can you use incomplete information about the frequency of bases on DNA strands to find the frequency of other bases?
The % of adenine in strand 1 is equal to the % of thymine in strand 2 and vice versa. The % of guanine in strand 1 is equal to the % of cytosine in strand 2 and vice versa. This is because of complimentary base pairing between the 2 strands.
How many hydrogen bonds are there between the 2 complimentary base pairings in DNA?
There are 2 Hydrogen bonds between Adenine and Thymine, and 3 Hydrogen bonds between Guanine and Cytosine
Why is semi-conservative replication important?
It ensures genetic continuity between generations of cells.
Why is DNA replication known as “semi-conservative”?
Each new DNA molecule consists of one strand from the parent DNA molecule, and one new strand.
Describe the process of semi-conservative DNA replication.
- DNA helicase breaks hydrogen bonds between complementary bases, unwinding the double helix
- Both strands act as template strands.
- Free DNA nucleotides in the nucleoplasm are attracted to exposed bases and join by complementary base pairing
- Hydrogen bonds form between complimentary base pairs (adenine-thymine and guanine-cytosine)
- DNA Polymerase moves along the polynucleotide chain, joining adjacent nucleotides on new strand by condensation reactions, forming phosphodiester bonds.
Why does DNA Polymerase move in opposite directions along the polynucleotide chains?
DNA has antiparallel strands, so the arrangements of nucleotides on each end are different. DNA Polymerase is an enzyme, and therefore has a specific active site, so it can only bind to substrate with a complimentary shape, which is the Phosphate end of each strand.
Which two scientists proposed models of the chemical structure of DNA and DNA replication?
Watson and Crick
Describe the work of Meselson and Stahl in validating the Watson-Crick model of semi-conservative DNA replication.
- Bacteria was grown in medium containing heavy nitrogen (15N), so nitrogen is incorporated into the DNA bases. The DNA was extracted & centrifuged, so it settled near the bottom, as all DNA molecules contain 2 heavy strands
- Bacteria that was grown in medium containing heavy nitrogen (15N) and was transferred to medium containing light nitrogen (14N) and was left to divide once - The DNA was extracted & centrifuged, so it settled in the middle, as all DNA molecules contain 1 original heavy strand and 1 new light strand
- Bacteria in light nitrogen (14N) was allowed to divide again.
The DNA was extracted & centrifuged, and half settled in middle, as
contains 1 original heavy and 1 new light strand; half
settles near top, as contains 2 light strands.
What components make up ATP?
A ribose sugar, Adenine and 3 Phosphate groups.
How is ATP broken down?
ATP is broken down via a hydrolysis reaction, using a molecule of water. ATP → ADP + Pi. This reaction is catalysed by the enzyme ATP Hydrolase
Give two ways in which the hydrolysis of ATP is used in cells
- The hydrolysis of ATP releases energy, so this energy can be used to provide energy for energy requiring reactions within cells.
- The hydrolysis of ATP releases an inorganic phosphate, which can be used to phosphorylate other molecules in the cell, making them more reactive.
How is ATP is resynthesised in cells?
ADP + Pi → ATP. This is a condensation reaction, and therefore releases a molecule of water. This is catalysed by the enzyme ATP Synthase and it occurs during respiration and photosynthesis.
Suggest how the properties of ATP make it a suitable immediate source of energy for cells
- Releases energy in small, manageable amounts
- Hydrolysis of ATP is a single reaction as only one bond is hydrolysed to release energy. This means that the energy is released immediately.
- ATP molecules can not exit the cell
Explain how hydrogen bonds occur between water molecules
Water is a polar molecule. The slightly negatively charged oxygen atoms attract the slightly positively charged hydrogen atoms of other water molecules.
Explain the Specific Heat Capacity of Water
Due to the Hydrogen bonding, water molecules take more energy to separate them, so the boiling point is higher than expected. As water therefore has a higher specific heat capacity, it is a buffer to sudden temperature changes. This is important when organisms are mostly water
Explain the Latent Heat of Vaporisation of Water
The Hydrogen Bonding also means that a lot of energy is required to evaporate 1kg of water. This means that sweat in mammals is a very efficient way of cooling as body heat is used to evaporate water.
Explain Cohesion and Surface Tension in Water
Cohesion allows water to be pulled through tubes e.g. xylem vessels. Where water molecules meet the air, they are pulled back to the body of water, resulting in surface tension. This allows water to support small organisms.
Give 3 ways that water is important to living organisms
- Metabolite - Water is used in hydrolysis and released in condensation, as well as it being a raw material in photosynthesis
- Solvent - Water dissolves gasses, wastes, ions and small hydrophilic molecules.
- Other - Evaporation cools organisms, isn’t easily compressed so allows turgor in plants, transparent so aquatic plants can photosynthesise.
Describe the role of Hydrogen ions
They maintain pH levels in the body, therefore affecting enzyme action.
Describe the role of Iron ions
They are a component of haemoglobin, therefore allowing oxygen to bind for transport as oxyhaemoglobin.
Describe the role of Sodium ions
They are involved in the co-transport of glucose and amino acids into cells. They are also involved in action potentials in neurons and they affect the water potential of cells, causing osmosis into and out of the cell.
What is Observational Research?
A research method in which data is collected by watching participants’ behaviour
Give 2 strengths of observational research.
- Observational research often produces valid results as we can investigate how people actually behave, rather than how they said they would, like in self report methods.
- Observations can be used when it would be unethical or impractical to manipulate the Independent Variable.
Give 2 weaknesses of observational research.
- Difficult to replicate as the way people act in a certain scenario may not be exactly the same every time.
- Results may be affected by observer bias, reducing the validity of the results.
What is a structured observation?
An observation in which observers collect data by recording the frequency of predetermined behaviours using a coding scheme.
Give 2 strengths of structured observations.
- Produces quantitative data which is easy to analyse and compare between conditions
- More objective and reduces chance of observer bias
Give 2 weaknesses of structured observations.
- May produce invalid results as the behaviours recorded may not be representative of all behaviours that could occur
- Produces quantitative data which lacks detail, therefore doesn’t provide detail and reasons for behaviour
What is an unstructured observation?
An observation in which observers collect data by writing down all behaviour that occurs in the observation period
Give 2 strengths of unstructured observations.
- Collects qualitative data which is rich in detail and can explain reasons for behaviour
- Unlike in structured observations, all behaviours will be recorded, so the results will be more valid
Give a 2 weaknesses of unstructured observations.
- As observers are recording everything that occurs, they may miss certain behaviours, therefore decreasing the reliability of results.
- Collects qualitative data, which is difficult to analyse and can be subjective, decreasing the validity of conclusions made.
What is a controlled observation?
An observation carried out in a controlled environment in which extraneous variables can be controlled, for example a laboratory.
Give 2 strengths of controlled observations
- High levels of control over extraneous variables, so causality can be established
- Can be replicated easily, so they have high external reliability.
Give 2 weaknesses of controlled observations
- Low ecological validity as the environment is highly artificial
- Participants are more likely to show demand characteristics, decreasing the validity of the results
What is a naturalistic observations?
An observation which takes place in the participants’ natural environment
Give 2 strengths of naturalistic observations
- More ecologically valid as the environment is natural.
- Participants are less likely to show demand characteristics, increasing the validity of the results
Give 2 weaknesses of naturalistic observations
- Low levels of control over extraneous variables, so it is difficult to establish causality
- Can not be replicated easily, so they have low external reliability.
What is a participant observation?
An observation where the observer takes part in the situation they are observing and becomes part of the observed group
Give 2 strengths of participant observations
- Observer can gain a more in-depth understanding of the participants’ behaviour as they are interacting with them
- The observer will understand the situation that they are observation better because they take part in it themself.
Give 2 weaknesses of participant observations
- Observer will likely have to record behaviours afterwards, and therefore may forget some behaviours, decreasing the reliability of results
- May lead to observer bias as the researcher is interacting with the participants
- Usually involves deceiving participants, and therefore is unethical
What is a non-participant observation?
An observation in which the observer doesn’t participate in the situation that they are observing and does not become part of the observed group
Give 2 strengths of non-participant observations
- Less likely to result in observer bias as the researcher does not interact with the participants
- Observer can record behaviours as they happen, therefore not relying on memory
Give 2 weaknesses of non-participant observations
- It may be difficult to understand behaviour of participants if the observer doesn’t interact with them
- The observer may not understand the situation they are observing if they do not participate in it
What is a covert observation?
An observation in which the participants are not aware that they are being observed
Give a strength of covert observations
Reduces the chance of demand characteristics, increasing the validity of results.
Give a weakness of covert observations
They are unethical as participants do not give informed consent