Proteins Flashcards

1
Q

What 2 functional groups does an amino acid have?

A

an amino group (NH2)

a carboxylic acid group (COOH)

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2
Q

What forms do proteins consist of only?

A

L forms (left)

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3
Q

Give an example of an amino acid with an acidc R group.

A

Aspartic acid

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4
Q

Give an example of a basic amino acid.

A

arginine

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5
Q

Give an example of an uncharged polar amino acid.

A

glutamine

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6
Q

Give an example of a polar amino acid.

A

glycine, alanine

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7
Q

How is a peptide bond formed?

A

condensation reaction

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8
Q

What is meant by the ‘primary structure’ of a protein?

A

the sequence of amino acids

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9
Q

How many different types of amino acid are there?

A

20

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10
Q

What is meant by the ‘secondary structure’ of an amino acid?

A

spatial arrangement of amino acid residues that are near each other in the linear sequence

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11
Q

What are the 2 forms the secondary structure can take?

A

alpha helix

beta pleated sheets

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12
Q

How is the shape of the alpha helix maintained?

A

by hydrogen bonds between C=O group and N-H group

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13
Q

What is meant by the ‘tertiary structure’ of a protein?

A

the spatial arrangement of amino acid residues that are FAR APART in a linear sequence

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14
Q

What are the 5 ways that the tertiary structure is maintained? (Bonding)

A
  • van der waals
  • hydrogen bonding
  • ionic interactions
  • disulphide bridges (between cysteine residues)
  • hydrophobic interactions
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15
Q

What is meant by the ‘quaternary structure’ of a protein?

A

the spatial arrangement of individual polypeptide chains in a multi-subunit protein

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16
Q

What is an example of a complex with a quaternary structure?

A

haemoglobin

17
Q

What structures of protein are affected by denaturation?

A

secondary and tertiary

18
Q

Why is primary structure of protein not affected by denaturation?

A

the reactions aren’t strong enough to break the peptide bonds

19
Q

Give 2 examples of causes of denaturation of proteins.

A

acids

heat

20
Q

What are some examples of the effects of denaturation? (4)

A
  • decreased solubility
  • altered water binding capacity
  • loss of biological activity
  • improved digestibility
21
Q

What do peptidases do?

A

cleave peptide bonds

22
Q

What do endopeptidases do?

A

cleave internal bonds of protein

23
Q

What do exopeptidase do?

A

cleave away one amino acid at a time

24
Q

What do carboxypeptidases do?

A

cleave at COOH terminal

25
Q

What do amino peptidases do?

A

cleave at NH2 terminal