1.4 - Proteins Flashcards

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1
Q

What is the general structure of an amino acid?

A
  • COOH carboxylic acid group
  • NH2 amine group
  • R variable region consisting of carbon chains & other functional groups
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2
Q

Describe how to test for proteins in a sample.

A

Use the Biuret test which confirms the presence of a peptide bond.
1) To make test solution alkaline, add a few drops of sodium hydroxide solution.
2) Add copper (II) sulfate solution.
Negative result: solution remains blue
Positive result: solution changes to purple

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3
Q

How many amino acids are there and how do they differ from one another?

A

20
Only differ in R group

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4
Q

How do dipeptides and polypeptides form?

A

Condensation reaction forms peptide bonds whilst releasing a water molecule.
Dipeptide = 2 amino acids
Polypeptide = 3 +

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5
Q

How do dipeptides and polypeptides form?

A

Condensation reaction forms peptide bonds whilst releasing a water molecule.
Dipeptide = 2 amino acids
Polypeptide = 3 +

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6
Q

What are the levels of protein structure?

A

Primary, secondary, tertiary & quaternary

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7
Q

Define ‘primary structure’ of a protein.

A

Primary structure is the sequence, number & type of amino acids in the polypeptide chain.
Determined by sequence of codons on mRNA

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8
Q

Define ‘secondary structure’ of a protein.

A

Hydrogen bonds form between amino acids in the polypeptide chain, automatically making it coil into an alpha helix, or fold into a beta pleated sheet.

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9
Q

Define ‘tertiary structure’ of a protein.

A

Hydrogen & ionic bonds, and disulfide bridges form between parts of the polypeptide chain.

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10
Q

Describe disulfide bridges in the tertiary structure of proteins.

A

Strong covalent S-S bonds between molecules of the amino acid cysteine

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11
Q

Describe ionic bonds in the tertiary structure of proteins

A

Relatively strong bonds between charged R groups.
pH changes causes ionic bonds to break.

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12
Q

Describe hydrogen bonds in the tertiary structure of proteins.

A

Numerous & easily broken.

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13
Q

Define ‘quaternary structure’ of a protein.

A

Some proteins are made of several polypeptide chains held together by bonds. The quaternary structure is the protein’s final 3D structure.

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14
Q

Describe the structure of globular proteins.

A
  • Spherical & compact
  • Hydrophilic R groups face outwards & hydrophobic R groups face inwards, so usually water soluble
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15
Q

Describe the function of globular proteins.

A

Involved in metabolic processes (e.g. enzymes & haemoglobin)

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16
Q

Describe the structure of fibrous proteins.

A

Can form long chains of fibres
Insoluble in water

17
Q

Describe the function of fibrous proteins.

A

Useful for structure & support (e.g. collagen in skin)

18
Q

Outline how chromatography could be used to identify the amino acids in a mixture.

A

1) Use capillary tube to spot mixture onto pencil origin line & place chromatography paper in solvent.
2) Allow solvent to run until it almost touches other end of paper. Amino acids move different substances based on relative attraction to paper & solubility in solvent.
3) Use revealing agent or UV light to see spots.
4) Calculate retention factor (Rf) values & match database.

19
Q

How is the retention factor value calculated in chromatography?

A

By dividing the distance travelled by the component by the distance travelled by the solvent.

20
Q

What are enzymes?

A

Biological catalysts that are responsible for speeding up metabolic reactions both at a cellular level and for the organism as a whole (intra & extracellular)

21
Q

Explain the induced fit model of enzyme action.

A

Shape of active site isn’t directly complementary to substrate, but is flexible.
As the substrate binds, the active site changes shape slightly in order to form an enzyme-substrate complex.
This puts strain on bonds in the substrate, lowering activation energy.

22
Q

How have models of enzyme action changed?

A

Initially lock & key model: rigid shape of active site complementary to only 1 substrate.
Now, induced fit model: also explains why binding at allosteric sites can change shape of active site.

23
Q

How could a student identify the activation energy of a metabolic reaction from an energy level diagram?

A

Difference between free energy of substrate & peak of curve.

24
Q

Name 5 factors that affect enzyme activity.

A
  • Enzyme concentration
  • Substrate concentration
  • Concentration of inhibitors
  • pH
  • Temperature
25
Q

How does substrate concentration affect rate of reaction?

A

The higher the substrate concentration, the faster the rate of reaction, as increases the chance of collisions between enzymes & substrates.
Only true up until ‘saturation’ point, when enzyme concentration becomes a limiting factor, as all active sites are full.
Substrate concentration naturally decreases with time as reactions take place, as they are used up. So therefore, rate of reaction will also decrease.

26
Q

How does enzyme concentration affect rate of reaction?

A

The higher the enzyme concentration, the faster the rate of reaction, as there are more enzymes to collide and form E-S complexes.
If amount of substrate is limited, there will be more than enough enzymes to deal with all available substrates, so adding more enzymes has no further effect.

27
Q

How does temperature affect rate of reaction?

A

As temp rises, enzymes have more kinetic energy, so vibrate more, meaning they are more likely to collide and form E-S complexes.
After optimum temp, too much kinetic energy breaks bonds in the enzyme, changing active site shape. The enzyme is denatured.

28
Q

How does pH affect rate of reaction?

A

All enzymes have optimum pH value (in humans, mostly 7)
Above and below optimum pH, H+ & 0H- ions found in acids and alkalis can affect ionic & hydrogen bonds that maintain enzymes tertiary structure.
Active site changes shape, so enzyme denatures.

29
Q

Why is pepsin unlike most enzymes found in humans?

A

It has an optimum pH of 2, which is useful as it works in the stomach (acidic environment).

30
Q

What are competitive inhibitors?

A

Molecules similar in shape to that of the substrate,
Compete with substrate ti bind to active site,
But no reaction takes place.
Instead they block the active site,
So no substrate can fit in and form an E-S complex.

31
Q

How does concentration of competitive inhibitors affect rate of reaction?

A

Depends on relative concentration of competitive inhibitors to substrate.
Higher conc of inhibitor = most active sites blocked.
Higher conc of substrate = most active sites are joined in E-S complexes to substrate.
However, competitive inhibitors only temporarily block active sites, as are released.

32
Q

What are non-competitive inhibitors?

A

Molecules that bind to allosteric site of enzymes (away from active site),
Causing active site to change shape,
So substrate molecules can no longer bind to it.
They have a different shape to the substrate.

33
Q

How does the concentration of non-competitive inhibitors affect the rate of reaction?

A

Permanently cause the active site to change shape, so increasing conc of substrate won’t make a difference to reation rate, as they can no longer bind to active site.
Permanently lowers rate of reaction.

34
Q

Contrast competitive and non-competitive inhibitors.

A

Competitive have similar shape to substrate, non don’t.
Competitive bind to active site, non bind to allosteric.
Competitive are released so are impermanent, non permanently change shape of enzyme.
Competitive’s effect decreases as substrate conc is added, non’s effect remains the same.

35
Q

Outline how to calculate rate of reaction from a graph.

A

Calculate gradient of line or gradient of tangent to a point.

36
Q

Outline how to calculate rate of reaction from raw data.

A

Change in concentration of product

37
Q

Why is it advantageous to calculate initial rate?

A

Represents maximum rate of reaction before concentration of reactants decreases & ‘end product inhibition’.

38
Q

What is ‘end-product inhibition’ ?

A

When the final product inhibits an enzyme involved in the initial reactions.