LEC06 Flashcards

Folding Proteins

1
Q

How many structure levels are proteins broken up into?

A

Four.

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

What is included in the primary structure?

A
  • Amino acid sequence
    • Drawn from amino acid end to the carboxyl end
    • Numbering starts from amino acid end
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is included in the secondary structure?

A
  • Local spatial arrangement of the polypeptide chain
  • Two regular arrangements
    • alpha helix; residuals stabilised by hydrogen bonds
    • beta sheet; adjacent segments stabilised by
      hydrogen bonds
  • Regular repeating structures are hydrogen bonded
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is included in the tertiary structure?

A
  • Overall 3D shape
  • Results from non-covalent interactions between amino acids and side chains (R)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is included in the quaternary structure?

A
  • Assembly of the polypeptide chain
    • Can be identical or different in sequence
  • The alpha and beta represent that the polypeptides have different primary structures
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What does myoglobin do?

A
  • Stores and transports oxygen to muscle cells
  • Important for aquatic animals so they can store air underwater
  • Single polypeptide monomer
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What does haemoglobin do?

A
  • Transports oxygen through veins and arteries
  • In red blood cells
  • Heme group is attached to polypeptide by non-covalent bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly