Topic 2/7/8 - Part 1 - Pictures/Diagrams Flashcards
Draw D-ribose
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Draw Alpha-D-glucose
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Draw Beta-D-glucose
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Draw a saturated fatty acid
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Draw an amino acid
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Identify the biochemical
Carbohydrate (starch)
Identify the biochemical
Lipid (triglyceride)
Identify the biochemical
Lipid (steroid)
**Make sure that you know this is a lipid
Identify the biochemical
Lipid (phospholipid)
**Make sure that you know this is a lipid
Identify the biochemical
Protein
The following diagram shows an exergonic reaction without an enzyme. Draw a corresponding diagram of the reaction when it is catalyzed by an enzyme.
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With the help of a graph, explain how temperature affects enzyme activity
- Low temperatures result in insufficient thermal energy for the activation of an enzyme-catalysed reaction to proceed
- Increasing the temperature will increase the speed and motion of both enzyme and substrate, resulting in higher enzyme activity
- This is because a higher kinetic energy will result in more frequent collisions between the enzymes and substrates
- At an optimal temperature (may vary for different enzymes), the rate of enzyme activity will be at its peak
- Higher temperatures will cause enzyme stability to decrease, as the thermal energy disrupts the enzyme’s hydrogen bonds
- This causes the enzyme (particularly the active site) to lose its shape, resulting in the loss of activity (denaturation)
With the help of a graph, explain how pH affects enzyme activity
- Changing the pH will alter the charge of the enzyme, which in turn will alter protein solubility and overall shape
- Changing the shape or charge of the active site will diminish its ability to bind the substrate, abrogating enzyme function
- Enzymes have an optimal pH (may differ between enzymes) and moving outside this range diminishes enzyme activity
With the help of a graph, explain how substrate concentration affects enzyme activity
- Increasing substrate concentration will increase the activity of a corresponding enzyme
- More substrates mean there is an increased chance of enzyme and substrate colliding and reacting within a given period
- After a certain point, the rate of activity will cease to rise regardless of any further increases in substrate levels
- This is because the environment is saturated with substrate and all enzymes are bound and reacting (Vmax)
Draw a diagram to demonstrate competitive inhibition
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Draw a diagram to demonstrate non-competitive inhibition
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Draw a graph of the reaction without inhibition, with competitive inhibition and with non-competiive inhibition and explain the trends
competitive inhibition:
- with increased substrate concentration, the maximum rate of the unhibited enzyme can be achieved; however it takes a much higher coentration of substrate to acheive this maximum rate
non-competitive inhibition:
- the enzyme cannot reach the same maximum rate because the binding of the non-competitive inhibitor prevents some of the enzymes from being able to react regardless ofo the substrate concentration
Identify the reaction as exergonic or endergonic
exergonic
Identify the reaction as exergonic or endergonic
endergonic
With the help of a diagram and with reference to threonine, explain end-product inhibition
- Through a series of five reactions, the amino acid “threonine” is converted to “isoleucine”
- As the concentration of isoleucine builds up, it binds to the allosteric site of the first enzyme in the chain (threonine deaminase), thus acting as a non-competitive inhibitor
Draw a diagram to illustrate the polar property of water and hydrogen bonding.
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Annotate a diagram of the condensation reactions between monosaccharide monomers to form disaccharides
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Identify the sugar
Cellulose
Identify which is starch and which is cellulose
Starch
