Proteins Flashcards

biological molecules - AQA - topic 1

You may prefer our related Brainscape-certified flashcards:
1
Q

Elements in protein

A
  • Carbon
  • Hydrogen
  • Oxygen
  • Nitrogen
  • Sometimes sulfur
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are proteins made of

A

Amino acids

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

What are proteins

A

Proteins are polymers made up of the monomer amino acids

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

Describe how amino acids are joined together to make a dipeptide

A
  • 2 amino acids join in a condensation reaction
  • Water is removed
  • peptide bonds are formed between OH of carboxyl and H of amine group
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

2 ways in which protein can be hydrolysed

A
  • heat w an acid
  • use enzyme protease at optimum temperature
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Primary structure

A

SEQUENCE of amino acids in a polypeptide chain

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

Secondary structure

A
  • Sequence of amino acids that can be coiled to form alpha helix or folded into beta pleated sheets
  • Held by hydrogen bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Tertiary structure

A
  • Further folding and coiling of the secondary structure
  • form a unique and specific 3D structure
  • held in place by hydrogen, ionic and disulfide bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Location of ionic and disulfide bonds in the tertiary structure

A

Between the R groups

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

Globular proteins

A
  • Soluble
  • Highly folded and coiled polypeptide chains
  • produce a complex and compact tertiary structure
  • Globular structure include enzymes and antibodies
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Quaternary structure

A
  • More than 1 polypeptide chain
  • held together by ionic, hydrogen bonds and SOMETIMES disulfide.
  • E.g. haemoglobin is made up of 4 polypeptide chains
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the denaturation of proteins

A
  • Alteration in the tertiary structure of the proteins
  • Irreversible
  • No longer functional
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Conditions of a denaturation of a protein

A
  • Caused by breaking of hydrogen and ionic bonds (not disulfide bonds because they remain unbroken at 70’)
  • Caused by high temperature above room temperature
  • Extreme changed in pH’s
  • Heavy metals (lead,copper,zinc)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What might cause a change in an amino acid sequence

A

Mutations - change in DNA sequence might code for different amino acids therefore primary structure changes

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

Explain how a change in the primary structure of a globular protein may result in a different 3D shape

A
  • Changes in the sequence of the amino acids
  • Bonds formed in different place
  • Changes in the tertiary structure which given protein its function
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Test for proteins

A

BIURET TEST
- add biuret reagent in a sample
- purple indicates protein
- blue indicates no protein