1.6- proteins Flashcards

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

what combines to form proteins?

A

polypeptides

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

amino acids

A

monomers from which proteins are made

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

structure of amino acids

A

amino group (-NH2)
carboxylic acid group (-COOH)
hydrogen group (-H)
R group (carbon containing chain)

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

How many different amino acids are there?

A

20- each determined by R groups

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

How are amino acids combined?

A

peptide bonds formed in condensation reaction

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

How can the peptide bond of a dipeptide be broken down to give 2 constituent amino acids?

A

hydrolisis

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

dipeptide

A

contains 2 amino acids

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

polypeptide

A

contains three or more amino acids

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

Through a series of condensation reactions, many amino acid monomers can be joined together in a process called…

A

polymerisation

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

Describe the primary structure of a protein

A

Primary structure of a protein is the order and number of amino acids in a protein. This
primary structure contains the initial sequence of amino acids and will therefore
determine the proteins function in the end.

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

Describe the secondary structure of proteins

A

shape which the polypeptide chain forms as a result of hydrogen bonding. This is most often a spiral known as alpha helix or beta pleated sheet-

hydrogen has slight positive charge whilst oxygen slight negative charge, as a result weak hydrogen bonds form= different structure eg a helix/ beta sheets

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

Describe the tertiary structure of proteins

A

3D shape of the protein and is formed from further
twisting and folding. A number of different bonds maintain the structure, these are:
- Disulfide bridges - these are strong and not easily broken.
- Ionic bonds - form between the carboxyl and amino groups that are not involved in
the peptide bond. They are easily broken by pH and are weaker than disulfide
bridges.
- Hydrogen bonds - numerous and easily broken

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

Describe the quaternary structure

A

arises from the combination of a number of polypeptide chains and associated non- protein groups into a large, complex protein molecule e.g haemoglobin

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

globular proteins

A

enzymes are compact

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

fibrous proteins

A

eg keratin, long and thus can be used to form fibres

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

what is the name for the test in proteins

A

Biuret test- detects peptide bonds

17
Q

describe the Biuret test

A
  1. Place the sample to be tested in a test tube and add an equal volume of sodium
    hydroxide at room temperature.
  2. Add a few drops of very dilute (0.05%) copper (II) sulfate soliton and mix gently.
  3. A purple colouration indicates the presence of a peptide bond and hence a protein. A
    negative result would mean the solution remains blue.