Protein Structure Flashcards

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

What are all proteins made up of?

A

Polymers of amino acids

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

How many types of amino acids are there?

A

20 different amino acids

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

How many different amino acids can plants make?

A

Plants can make all 20 types of amino acids whereas animals can only make some. They obtain others through their diet.

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

What is the general structure of an amino acid?

A

Amine group -NH2
Carboxylic acid group -COOH
Hydrogen -H
Residual group

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

How is a dipeptide formed?

A

Two amino acids monomers undergo a condensation reaction. A peptide bond forms between the two units producing a dipeptide and a water molecule.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What is the primary structure of a protein?

A

Many amino acid molecules are joined together by peptide bonds during condensation reactions.
This creates a long chain of amino acids called a polypeptide chain.
A protein is made up of one or more polypeptide chains.

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

What reaction can break the peptide bond?

A

Hydrolysis reaction

Water reacts with the joined amino acids.

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

Functions of proteins

A

Hormones
Enzymes
Antibodies
Components of cell membranes

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

What are the two structures made in the secondary structure of a protein?

A

Alpha Helix
Beta pleated sheet
One protein may contain both structures or one.

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

What bonds are formed in a alpha helix structure?

Where do they form?

A

Hydrogen bonds form between the NH (amine group) and the C=O (carboxylic acid.
The H bonds stabilise the helix shape.

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

What bonds are formed in a beta pleated sheet structure? Where do they form?

A

Hydrogen bonds hold parallel chains between several polypeptide chains.

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

The type of bonding in the tertiary structure of the protein is dependent on…

A

The r-groups within the polypeptide chains

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

What chemical bonding occurs in the tertiary structure?

A

Disulphide bridging - Sulphur R groups
Ionic bonding - Between ionised R groups
Hydrogen bonding- alpha helix and beta pleated sheet

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

The chemical bonding in the tertiary structure work to..

A

Polypeptide chains bend and fold to give a precise 3D shape.

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

What maintains the final tertiary structure of the protein?

A

Chemical bonds and the hydrophobic interactions between the R groups

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

Characteristics of a polar R-group

A
  • e- not shared evenly through molecule
  • Attracted to other polar molecules e.g. water
  • Hydrophilic
17
Q

Characteristics of non-polar R group

A
  • Hydrophobic
  • Repel water
  • Non-polar R-groups arranged to face the inside of the protein to exclude water from the centre of molecule
18
Q

What proteins have a quaternary structure?

A

A protein made up of several polypeptide chains.

Single chain proteins stop at the tertiary structure.

19
Q

Examples of proteins with a quaternary structure

A

Haemoglobin; 4 polypeptide chains held tightly together

20
Q

Why is the primary structure important?

A

The amino acids join together in a chain
The order determines the position of the bonds, the folding of the protein into its 3D structure and its properties, in the tertiary structure.

21
Q

What is a conjugated protein?

A

.

22
Q

What are the two groups of proteins?

A

Globular

Fibrous

23
Q

What shape do globular proteins fold into?

A

Polypeptide chains fold into a compact spherical shape.

Soluble

24
Q

Globular proteins are soluble/insoluble? Why?

A

Soluble

Hydrophilic side chains project out of the molecule, attracting water molecules. - important for metabolic reactions

25
Q

Examples of globular proteins

A

Transport proteins; haemoglobin, myoglobin (oxygen store in muscles)
Antibodies: precise active site for microorganisms
Enzymes: catalyse reactions

26
Q

How does the structure of a globular protein relate to their function?

A

The three dimensional structure of the globular protein is crucial to their roles of binding to other substances.
The specific shape is formed to create an active site allowing specific substrate molecules to attach.
Important to form enzyme substrate complexes and to catalyse reactions in cells.

27
Q

What is the shape of a fibrous protein?

A

Polypeptide chains remain as long chains to be used as structural molecules.
Several polypeptide chains can be cross linked for extra strength. (H bonds)

28
Q

Are fibrous proteins soluble or non-soluble?

A

Insoluble

29
Q

Examples of fibrous proteins

A

Keratin - hair and skin

Collagen (3 chains, H cross links) - blood vessel walls, skin, tendons

30
Q

How does the structure of fibrous proteins relate to their function?

A

Several chains joined by strong H bonds create strength required to create blood vessels and hair

31
Q

How does the primary structure of a protein affect the tertiary structure? [4 marks]

A

The primary structure determines the order of amino acids and their r-groups in the polypeptide chain.
This order determines the type of bonding which occurs, causing the protein to fold into a specific shape.
The types of bonding which may form; H, ionic and di-sulphide bridging