1.3 - Proteins Flashcards

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1
Q

Draw the general structure of an amino acid

A
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2
Q

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

A

Peptide bond

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3
Q

How is a dipeptide formed?

A

Condensation of two 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

The 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 hydrogen bonding

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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
Lilac

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11
Q

What is an enzyme?

A

Biological catalysts that increase the rate of reaction by lowering the activation energy and providing an alternate reaction pathway

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12
Q

Describe the induced fit model of enzyme action

A

Substrate binds to active site - ESC forms
Active site changes shape to it is complementary to substrate
Bonds are broken and formed in substrate

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13
Q

Why are enzymes referred to as specific?

A

They have 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 concentration increases rate of reaction increases, until it plateaus due to other limiting factor e.g enzyme concentration

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16
Q

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

A

Higher concentration of competitive inhibitor means a slower rate of reaction
Rate can be increased by increasing substrate concentration

17
Q

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

A

Higher concentration of non-competitive inhibitor means slower rate of reaction
Rate cannot be increased by increasing substrate concentration

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)
So active site and substrate no longer complementary so no substrate can bind

20
Q

Describe lock and key enzyme model

A

The enzyme and substrate fit together perfectly and form an ESC