Proteins 1 Flashcards

(34 cards)

1
Q

What occurs during protein synthesis?

A
  • DNA transcribed to RNA

- RNA translated to protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Codon

A

Chain of three bases which code for an amino acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is a codon defined by?

A

The initial nucleotide from which translation starts

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the basic structure of an amino acid?

A

Central carbon with 4 bonds:

  • amino group
  • variable side chain
  • carboxylic acid group
  • hydrogen
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What are the different types of amino acids?

A
Aliphatic
Aromatic
Sulphur containing
Basic
Uncharged polar
Acidic
Other
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is a peptide bond?

A

Covalent bond between a carboxylic acid and amine group

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Where does the formation of peptide bonds occur?

A

Within a ribosome in during translation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What is a polypeptide chain?

A

A chain of two or more amino acids covalently bonded

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is the primary structure of a protein?

A

The sequence of amino acids in a polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is the source of versatility in a proteins structure and function?

A

The primary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What is the secondary structure of a protein?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What two structures are involved in secondary structure?

A

Alpha Helix

B Pleated Sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

How is the alpha helix structure held in place?

A

By hydrogen bonds between every N-H group and the O2 of the C=O group in the next turn of the helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

How is the beta pleated sheet structure held in place?

A

Held together by hydrogen bonds between the amide groups of linear polypeptide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What is the tertiary structure of a protein?

A

The spatial arrangement of amino acid residues that are far apart in a linear sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What forces are involved in the tertiary structure of a protein?

A
Van der Waals
Ionic interactions
Hydrogen bonds
Disulphide bridges
Hydrophobic interactions
17
Q

When do ionic interactions occur?

A

Between 2 close, oppositely charged R groups

18
Q

What are Van der Waals?

A
  • Non-specific, weak attractions between atoms 0.3-0.4 nm apart
  • They are individually weak but in a folded protein structure, a large number exist- thereby stabilising the structure
19
Q

What are hydrogen bonds?

A
  • Similar to Van der Waals but are stronger and permanent

- Occur when H is bonded to either O, N or F and a lone pair of electrons are present

20
Q

Name 2 substances that hydrogen bonding takes place in?

A

Water

Ammonia

21
Q

What are hydrophobic interactions?

A

Intra-polypeptide interactions which occur in an environment within proteins from which water is excluded

22
Q

Where are the hydrophobic R groups in globular water-soluble proteins?

A

Inside of the protein

23
Q

What makes a protein water soluble?

A

Hydrophilic R groups on the outside hydrogen bonding to water

24
Q

What are disulphide bridges?

A
  • Strong covalent bonds between two cysteine residues.
  • Common in extra-cellular proteins
  • Can occur between as well as within a polypeptide
25
What is the quaternary structure of a protein?
Refers to the spatial arrangement of individual polypeptide chains in a multi-subunit protein
26
What does the denaturation of proteins involve?
The disruption and possible destruction of both secondary and tertiary structures
27
Why does the primary structure remain the same after denaturation?
Denaturation reactions are not strong enough to break the peptide bonds
28
What can cause denaturation?
- Acids - Heat - Solvents (ethanol, methanol) - Cross linking reagents (formaldehyde) - Chaotropic agents (urea) - Disulphide bond reducers (2 mercaptoethanol)
29
What are the effects of denaturation?
- Decreased solubility - Altered water binding capacity - Loss of biological activity - Improved digestibility
30
What are peptidases responsible for?
Cleavage of peptide bonds
31
What are endopeptidases responsible for?
Cleavage of internal bonds
32
What are exopeptidases responsible for?
Cleavage of one amino acid at a time
33
What are carboxypeptidases responsible for?
Cleavage at -COOH terminal
34
What are aminopeptidases responsible for?
Cleavage at -NH2 terminal