What I reckon is that you should check your answers - then try the test again at a later date - keep going until you get all these questions right.

 

Give an example of a monosaccharide Glucose, Fructose (check notes for others)
Give an example of a disaccharide Maltose, Lactose, Sucrose (check notes for others)
Give an example of a polysaccharide Starch, Glycogen, Cellulose (check notes for others)
How many carbon atoms are there in a glycerol molecule 3
Which biological molecule has glycerol in its structure lipid/phospholipid
What's the name of the bonds that hold saccharide molecules together in carbohydrates glycosidic
What's the name of the bonds that hold amino acids together peptide
What type of chemical reaction occurs when two monosaccharides join to form a disaccharide condensation
Which of these is an atom:
  • H2O
  • CO2
  • C
  • C6H12O6
C
What type of chemical reaction occurs when a triglyceride is broken into glycerol and fatty acid molecules. hydrolysis
In which molecule would you find ester bonds? lipid
What is the main additional element present in proteins but not carbohydrates or lipids nitrogen
Describe how you could perform a test to detect the presence of lipids dissolve in ethanol - decant into water - cloudy emulsion = lipid present
What level of protein structure determines the overall three dimensional shape of a polypeptide? tertiary structure
What feature do carbohydrates and proteins have in common that lipids do not have. they can form polymers/long chain molecules
Give one function of triglyceride fats in living organisms energy storage (check notes for others)
What is the name of the reagent used in the protein test? Biuret
How many carbon molecules are there in a molecule of glucose 6
When seperating a mixture of amino acids using chromatography what properties of the amino acids cause them to seperate on the chromatography paper? molecular size - solubility in the solvent
The presence of what turns iodine blue/black? starch
   
How many micrometres in a millimetre 1,000
Give the main functions of the following organelles:
  • Mitochondrion
  • Chloroplast
  • Nucleus
  • RER
  • Ribosomes
  • SER
  • Golgi Apparatus
  • Cell Membrane
Mitochondrion site of ATP synthesis/aerobic respiration
Chloroplast site of photosynthesis
Nucleus controls the cells reactions/contains genetic material
RER polypeptide isolation and transport
Ribosomes site of polypeptide synthesis
SER synthesis and transport of lipids
Golgi Apparatus final stages of protein assembly and transport of proteins
Cell Membrane controls entry and exit of substances in and out of the cell
What type of cells are bacteria prokaryotes
Give the advantages and disadvantages of using electron microscopes to view cells EM gives greater resolution, specimen cannot be alive
What are microvilli? infoldings of the cell membrane that increase surface area
Where does the construction of a polypeptide occur? at the ribosome
What might you find in a lysosome? digestive enzymes
What are the components of the fluid mosaic membrane proteins + phospholipids
Give two functions of proteins in membranes transport, receptor, membrane bound enzyme
If you were using centrifugation to seperate cell organelles from a mixture which organelles would you expect to sediment out first? the nuclei
   
Through which part of the membrane do things move by active transport? the proteins
What is meant by the term osmosis the movement of water across a biological membrane from an area of less negative to an area of more negative water potential
Give two differences and one similarity between facillitated diffusion and active transport similarity = both use proteins to cross membrane

differences = active transport requires energy (ATP) facilitated diffusion does not, active transport is against the concentration gradient facilitated diffusion is with it.

If a plant cell has a WP of -560 kPa and an OP of -600 kPa, what would its wall pressure be? 40 kPa
If a red blood cell bursts when placed in a solution of distilled water (WP=0) Why doesn't a plant cell? because of it's cellulose cell wall
   
Why do small animals like shrews have to have a high metobolic rate to keep warm. because they have a large surface area to volume ratio therefore lose heat very easily
What feature do specialised gas exchange surfaces share large surface area, moist, thin (short diffusion distances), good vascular supply
Why is it more difficult to ventilate gills than lungs because water is more dense than air
Which muscles are involved in inspiration in humans the diaphragm and intercostal muscles
What keeps the trachea open in humans? cartilage
Why do desert plants have less stomata than plants found in marshy areas? because water is lost through stomata
In humans what is the path of an oxygen molecules from the mouth to the alveoli mouth - pharynx - larynx - trachea - bronchi - bronchiole - alveoli
What is the main cause of expiration in humans? elastic recoil of lung tissue
What are the main gas exchange structures in bony fish? the secondary lamellae of the gills
   
Explain what happens to an enzyme molecule when it is denatured by high temperatures. H-bonds between polypeptides broken, tertiary structure changed, shape of active site changed, therefore substrate no longer fits active site
Why does an enzyme only speed up one (or at the most a few) different chemical reaction(s)? because active site is a specific shape only one (a few) molecules can fit into it
How do enzymes speed up the rate of chemical reactions by lowering the activation energy required
Describe the effect of increasing substrate concentration on the rate of an enzyme controlled reaction as substrate concentration increases the rate of reaction increases
Why would increasing the temperature from 15 to 25 degrees increase the rate of an enzyme controlled reaction between 15 and 25 degrees the amount of kinetic energy increases therefore the number of successful collisions (between substrate and enzyme) per unit time increases
Using you knowledge of enzyme structure explain how a non-competitive inhibitor works it binds at a site other than the active site causing a change to the enzymes tertiary structure - therefore changing the shape of the active site so the substrate can no longer fit.

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