1.6 Proteins Flashcards

1
Q

What are proteins made up of

A

Amino acids

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

Describe the structure of an amino acid (like the groups in the amino acid)

A

*Amine group (NH2) on the left
* Carboxyl group on the right (C=OOH)
* R group/ variable group at the top
and a C and a H below the carbon

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

Describe how amino acids are joined together to form a dipeptide

A
  • Condensation reaction
  • Water is removed
  • Peptide bond forms between OH of carboxyl and H of the Amine group
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What are proteins

A

Polymer made up of the monomer amino acids

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

What is the primary structure is

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
6
Q

What is the secondary structure

A
  • Folding (repeating patterns) of polypeptide chains e.g. alpha helix or beta pleated sheets
  • Due to hydrogen bonds between amino acids
  • between the NH and C=O
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is the tertiary structure

A

*Protein gets further foldings of the secondary structure
*Forming a unique 3D shape
*Held in place by Ionic, Hydrogen and disulphide bonds

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

Where do the ionic and Disuphide bonds form in the tertiary structure

A

Between the R groups of different amino acids

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

When do you get disulphide bonds

A

If both amino acids have sulphur in their R groups

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

Describe the quaternary structure of a protein

A

More than one polypeptide chain
Formed by interactions between polypeptides (hydrogen bonds ionic bonds and disulfide bridges)

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

What is an example of a quarternary structure protein

A

Haemoglobin

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

What happens if a protein denatures

A

The bonds which hold the tertiary structure and secondary structure break and therefore their unique shape is lost

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

What are the conditions that cause enzymes to denature

A

Too high a pH( too many H+ions or OH- ions)
Too high a temperature (too much kinetic energy)

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

What is the importance of the primary structure

A

If even one amino acid in the sequence changes it will cause the Ionic, Hydrogen or disulphide bond to form at a diff location resulting in a diff 3D shape

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

EXPLAIN HOW A CHANGE IN DNA BASE SEQUENCE CAN AFFECT AN ENZYME REACTION

A

Base sequence determines sequence of amino acids in polypeptide chain/primary structure
3 bases code for one amino acid
Primary structure determines position of bonds between R groups in the tertiary structure
Hydrogen, ionic bonds and disulphide bonds
A change in tertiary structure/ bonds changes shape of active site of the enzyme
Meaning the substrate can no longer bind to form an enzyme substrate complex

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