proteins and enzymes Flashcards

(26 cards)

1
Q

what is a protein?

A

a polymer made of monomers (amino acids)

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2
Q

what are the functional groups of an amino acid?

A
  • carboxylic acid (COOH)
  • amine group (H₂N)
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3
Q

what differs in all amino acids and why?

A

the R group which represents a side chain so that there are different types of amino acids

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4
Q

how many types of amino acids are there?

A

20

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5
Q

what type of bond forms when a condensation reaction occurs when forming a dipeptide?

A

a peptide bond between an amine group and a hydroxyl group from another amino acid

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6
Q

what are different levels of structures of proteins?

A
  1. primary structure
  2. secondary structure
  3. tertiary structure
  4. quaternary structure
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7
Q

describe the primary structure

A

the order and sequence of amino acids joined by a condensation reaction forming peptide bonds which determine the tertiary structure

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8
Q

describe the secondary structure

A
  • contains hydrogen bonds which are between amino acids
  • forms an alpha helix structure or beta pleated sheets
  • this makes the structure stable by forming a polypeptide
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9
Q

describe the tertiary structure

A
  • contains hydrogen, ionic and disulphide bridges bonds between the R groups
  • which forms 3D structure by the polypeptide chain folding
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10
Q

describe the quaternary structure

A

made up of many polypeptide chain forming a complex 3D structure

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11
Q

describe a method to test for proteins

A
  1. crush up food in a pestle and mortar
  2. add water to form a solution
  3. add biuret solution which detects a peptide bond present.
  4. shake and leave for 2 mins
  5. if proteins are present, it should turn from a blue –> lilac
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12
Q

what type of test is the biochemical test for protein?

A

qualitative

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13
Q

what are enzymes?

A

enzymes are made of proteins which lowers activation energy to speed up chemical reactions
- enzymes are used as catalysts

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14
Q

what do enzymes catalyse?

A

enzymes catalyse specific metabolic reactions at an intercellular level and a n extracellular level

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15
Q

what is an example of a intercellular reaction?

A

aerobic respiration

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16
Q

what is an example of an extracellular reaction?

17
Q

what is the induced fit model?

A
  • where the substrate collides with a enzyme
  • then the active site changes shape to fit around the substrate
  • which then forms an enzyme substrate complex
18
Q

what does inhibitors do?

A

prevents the substrate to bind to the enzyme

19
Q

what does non competitive inhibitors do?

A
  • they have a different shape to the substrate.
  • so they bind to the allosteric site
  • this changes the shape of the active site
  • so the substrate can no longer bind to the active site as they are no longer complementary
  • no more ES complexes formed
20
Q

what does competitive inhibitors do?

A
  • they have a similar shape to the substrate
  • they compete with the substrate to bind to the active site of the enzyme
  • the CI binds to the enzyme’s active site instead of the substrate
  • no more ES complexes formed
21
Q

what would increasing substrate conc do to an competitive inhibitor?

A

increasing the substrate conc will reverse effects of a competitive inhibitor as substrate out competes the CI

22
Q

what are the effects of rate of enzyme controlled reactions?

A

temperature, pH, enzyme concentration and substrate concentration

23
Q

what does temperature do to rate of enzyme controlled reactions?

A
  • the ke of the molecules increase
  • more enzyme substrate collisions
  • which increases the rate of reaction
  • so more ES complexes are formed
    optimum temperature
  • enzyme will denature
  • no substrate wouldn’t bind to enzyme as the active site changes shape
  • no ES complex formed
  • the reaction stops which is irreversible
24
Q

what does pH do to the rate of enzyme controlled reactions?

A
  • most enzymes work best at pH 7
  • when enzymes are above or below optimum pH, H and OH ions disrupt the tertiary structure (the bonds)
  • if the pH is extremely high, the enzyme denatures so the active site changes shape so no ES complex formed as substrate doesn’t fit
25
what does enzyme concentration do to the rate of enzyme controlled reactions?
- by increasing enzyme concentration, it increases the number of active sites - so more ES complexes can be formed - rate of reaction increases until substrate becomes the limiting factor (more enzyme than substrate) - by increasing enzyme conc even more, it won't affect rate as no more ES complex formed
26
what does substrate concentration do to the rate of enzyme controlled reactions?
- by increasing substrate concentration, it increases the number of active sites - so more ES complexes can be formed - rate of reaction increases until enzyme becomes the limiting factor (more enzyme than substrate) - by increasing substrate conc even more, it won't affect rate as no more ES complex formed