1.3 - Proteins Flashcards

1
Q

Draw the general structure of an amino acid

A
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2
Q

What is the bond formed between 2 amino acids in a condensation reaction?

A

peptide bond
between amine and carboxyl groups

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3
Q

How is a dipeptide formed?

A

condensation of 2 amino acids

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4
Q

How is a polypeptide formed?

A

condensation of many amino acids

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5
Q

3 types of bond that contribute to the tertiary structure of a protein (shape)

A
  • hydrogen bonds
  • ionic bonds
  • disulfide bridges
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6
Q

Describe the primary structure of a protein

A

amino acid sequence

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7
Q

Describe the secondary structure of a protein

A

2D folding of polypeptide chain as a result of H bonding
e.g beta-pleated sheet, alpha helix

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8
Q

Describe the tertiary structure of a protein

A

3D folding of a polypeptide chain due to interactions between R groups

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9
Q

Describe the quaternary structure of a protein

A

multiple polypeptide chains

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10
Q

Describe the Biuret test for proteins

A
  • add Biuret
  • positive: blue -> lilac
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11
Q

How does an enzyme increase rate of reaction?

A
  • lowers activation energy
  • induced fit causes active site to change shape
  • ESC complex causes bonds to weaken as they bend (and break)
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12
Q

Describe the induced fit model of enzyme action

A
  • substrate binds to active site, forming ESC
  • active site changes shape to now complementary to substrate
  • (H) bonds are broken and formed in substrate
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13
Q

Why are enzymes referred to as specific?

A

specific tertiary structure (active site) which is complementary to a specific substrate

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14
Q

Describe the effect of enzyme concentration on the rate of reaction

A

increasing enzyme concentration increases the rate of reaction

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15
Q

Describe the effect of substrate concentration on the rate of reaction

A

as substrate conc increases rate of reaction increases, until it plateaus due to other limiting factor e.g enzyme conc

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16
Q

Describe the effect of concentration of competitive inhibitors on the rate of reaction

A
  • higher conc of competitive inhibitor = slower rate of reaction
  • rate can be increased by increasing substrate conc
17
Q

Describe the effect of concentration of non-competitive inhibitor on the rate of reaction

A
  • higher conc of non-competitive inhibitor = slower rate of reaction
  • rate CANNOT be increased by increasing substrate conc
18
Q

Describe how a competitive inhibitor works

A
  • inhibitor similar shape to substrate
  • binds to active site
  • prevents ESC forming
19
Q

Describe how a non-competitive inhibitor works

A
  • attaches to enzyme at allosteric site
  • changes tertiary structure (active site)
  • active site and substrate no longer complementary so no substrate can bind
20
Q

Describe lock and key enzyme model

A

enzyme and substrate fit together perfectly and form an ESC

21
Q

Why would 2 proteins with same no. and type of amino acids have different tertiary structures?

A
  • different primary structures
  • so H bonds formed in different places