Topic 2/7/8 - Part 1 - Pictures/Diagrams Flashcards

1
Q

Draw D-ribose

A

Refer to picture

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Draw Alpha-D-glucose

A

Refer to picture

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Draw Beta-D-glucose

A

Refer to picture

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Draw a saturated fatty acid

A

Refer to picture

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Draw an amino acid

A

Refer to picture

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Identify the biochemical

A

Carbohydrate (starch)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Identify the biochemical

A

Lipid (triglyceride)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Identify the biochemical

A

Lipid (steroid)

**Make sure that you know this is a lipid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Identify the biochemical

A

Lipid (phospholipid)

**Make sure that you know this is a lipid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Identify the biochemical

A

Protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

The following diagram shows an exergonic reaction without an enzyme. Draw a corresponding diagram of the reaction when it is catalyzed by an enzyme.

A

Refer to picture

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

With the help of a graph, explain how temperature affects enzyme activity

A
  • 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)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

With the help of a graph, explain how pH affects enzyme activity

A
  • 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
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

With the help of a graph, explain how substrate concentration affects enzyme activity

A
  • 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)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Draw a diagram to demonstrate competitive inhibition

A

Refer to picture

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Draw a diagram to demonstrate non-competitive inhibition

A

Refer to picture

17
Q

Draw a graph of the reaction without inhibition, with competitive inhibition and with non-competiive inhibition and explain the trends

A

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
18
Q

Identify the reaction as exergonic or endergonic

A

exergonic

19
Q

Identify the reaction as exergonic or endergonic

A

endergonic

20
Q

With the help of a diagram and with reference to threonine, explain end-product inhibition

A
  • 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
21
Q

Draw a diagram to illustrate the polar property of water and hydrogen bonding.

A

Refer to picture

22
Q

Annotate a diagram of the condensation reactions between monosaccharide monomers to form disaccharides

A

Refer to picture

23
Q

Identify the sugar

A

Cellulose

24
Q

Identify which is starch and which is cellulose

A

Starch

25
Q

Identify the sugar

A

Amylose (starch)

26
Q

Identify the sugar

A

Amylopectin (starch)

27
Q

Identify the sugar

A

Glycogen

28
Q

Identify the sugar

A

Glucose molecule (Beta-D)

29
Q

Draw a labelled diagram to illustrate the formation of a triglyceride from gylcerol and fatty acids

A

Refer to picture

30
Q

Identify whether the following picture is a cis-fatty acid or a trans-fatty acid

A

Trans

31
Q

Identify whether the following picture is a cis-fatty acid or a trans-fatty acid

A

Cis

32
Q

Draw a labelled diagram to illustrate the formation of a polypetide from amino acids

A

Refer to picture