ppqs Flashcards

1
Q

Explain why increasing the temperature of an enzyme-controlled reaction changes the rate
of reaction

3 marks

A
  • higher kinetic energy
  • more enzyme substrate complexes made
  • enzyme active site will denature due to bond changes in the enzyme altering the active site
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2
Q

Describe how two named variables, other than the potato, can be controlled in order to
obtain valid results

4 marks

A
  • same volume of hydrogen peroxide
  • use a measuring cylinder/pipette
  • same temperature
  • thermostatically controlled water bath
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3
Q

Explain why the rate of reaction decreases over time

2 marks

A
  • less of enzyme-substrate complexes are formed
  • substrate is used up
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4
Q

Explain why adding citric acid to cut fruit reduces the rate at which the fruit turns brown.

2 marks

A
  • enzyme active site changes
  • acid affects the hydrogen bonds in enzyme
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5
Q

(ii) Give the meaning of the term tertiary structure of a protein.

2 marks

A
  • the folding of a protein to form a precise 3D shape
  • hydrogen ionic and disulfide bridges between R groups hold the structure together
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6
Q

Actinomycin D (act D) inhibits transcription.
Explain why pollen tubes could still grow in the presence of act D

2

A
  • plant still contains some mRNA that allows it to grow
  • some protein synthesis can take places
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7
Q

Cycloheximide inhibits translation.
Describe the process of translation.

4

A
  • mRNA attaches to ribosomes
  • tRNA attached to specific amino acid
  • tRNA anticodon binds to mRNA codon
  • peptide bonds form between amino acids
  • start and stop codons involved in the process
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8
Q

Describe how monomers are bonded to a polypeptide chain during the synthesis of actin.

2

A
  • through peptide bonds between monomers and polypeptide chain
  • through condensation reaction
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8
Q

Explain why water flows into the part of the cell where the soluble components are
located

2

A
  • water enters cell by osmosis
  • goes from a high water potential to a low water potential
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9
Q

Describe the events that take place resulting in T helper cell activation, following the
formation of pseudopodia by the macrophages

3

A
  • bacteria engulfed and digested
  • antigen attached to MHC antigen
  • macrophage becomes an antigen presenting cell
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10
Q

(i) Describe what is meant by the secondary structure of a protein.

2

A
  • folding of a primary to form an alpha helix or beta pleated sheet
  • formation of hydrogen bonds
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11
Q

(ii) Explain why the misfolded protein cannot be digested by some protease enzymes.

3

A
  • enzymes have active sites specific to certain amino acid sequences
  • misfolded protein will not bind to specific active site
  • enzyme is unable to hydrolyse peptode bond
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12
Q

Explain how the primary structure of a peptide hormone determines its properties

A
  • primary structures are a sequence of amino acids that determine the tertiary structure
  • because amino acids determine the position of the bonds
  • hydrogen bonds form between R groups
  • polar groups on outside to relate well with blood
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13
Q

Explain why the DNA base sequences coding for these three nonapeptides are more variable than their amino acid sequences.

3

A
  • the same amino acids have different bases that code for them
  • more triplet codes than amino acids
  • code is degenerate
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14
Q

Explain why this protein is soluble in water. (globular)

3

A
  • hydrophilic groups on outside to relate well with water
  • form hydrogen bonds with water
  • bc water is a polar solvent
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15
Q

Explain why the enzyme catalase is described as having a tertiary and quaternary structure.

3

A
  • tertiary bc primary protein is folded to form a precise 3D shape
  • quarternary bc 4 polypeptide chains arranged around a haem group
  • proteins with haem groups have a quarternary structure
16
Q

describe the structure of collagen

3

A
  • 3 polypeptide chains
  • arranged in a triple helix
  • held together by hydrogen bonds
16
Q

Explain how bacteria may become resistant to streptomycin if a mutation changes the primary structure of a protein

3

A
  • different R groups
  • therefore different secondary structure
  • different shaped ribosome
  • therefore streptomycin cannot bind
16
Q

describe the structure of a golbular protein

2

A
  • hydrophilic groups on the outside
  • tertiary structure
  • held together by hydrogen bonds
16
Q

Describe the tertiary structure of a globular protein.

3

A
  • folded into a 3D shape
  • hydrophilic groups on outside
  • hydrophobic groups on inside
  • held together by hydrogen bonds
17
Q

Explain the significance of repeating sequences of amino acids in the formation of tropocollagen

2

A
  • glycine is very small so the collagen fibres are very close together
  • this allows the formation of peptide bonds which hold the polypeptide chains together
17
Q

The base sequence of this polyphenol oxidase gene is different in this grape variety.
Explain how this leads to the production of inactive enzyme

3

A
  • different amino acid sequence
  • different R groups
  • secondary/tertiary structure is different
  • active site not complementary
18
Q
A
19
Q
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19
Q
A