Proteins Flashcards

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

What are amino acids?

A

the monomers from which proteins are made

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

How are dipeptides formed?

A

the condensation of 2 amino acids

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

How are polypeptides formed?

A

the condensation of many amino acids

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

How are peptide bonds formed?

A

a condensation reaction between 2 amino acids

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

What are proteins made up of?

A

one or more polypeptides

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

What is the amine group?

A

H2N

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

What is the carboxyl group?

A

COOH

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

What is the R group/ Variable group?

A

the 20 different options of amino acids that create the side chain - the only difference in amino acids

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

What is the primary structure?

A

the sequence of amino acids in the polypeptide chain
- determines the final shape and function

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

What is the secondary structure?

A

held together by hydrogen bonds between the carboxyl and amine group in the polypeptide backbone
- coil into alpha helix
= hydrogen bonds run parallel with long helical axis
= strong stable structure due to many hydrogen bonds
- polypeptide chain fold back on itself to form beta pleated sheets
= held together by hydrogen bonds

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

What is the tertiary structure?

A
  • final 3D structure formed by folding of polypeptide chains
  • each protein has unique tertiary structure which is responsible for its specific properties and functions
    e.g. enzymes active site
  • can be denatured by heat or pH - increased kinetic energy can break bonds - not reversible
  • held together by bonds between the R groups of the amino acids so depends on the sequence of the amino acids
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What are the bonds in the tertiary structure?

A

hydrogen
- between slightly oppositely charged groups - forms slightly negative charge
- can be split by high temp of altered pH (weak)

ionic
- form between basic + acidic group
- between oppositely charged R groups
- can be split by changing pH (strong)

disulphide
- between 2 cysteine aa - covalent S-S
- can be split by reducing agents (strongest)

Van der Waal forces (extra reading)
- weak forces of attraction between non polar groups
- water excluded from hydrophobic side chains - helps keep side chains together
- split by rise in temp

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

What is the quaternary structure?

A
  • only found in proteins containing more than 1 polypeptide
    e.g. haemoglobin - 4 globular arranged in tetrahedral structure
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

The final 3D structure can be?

A

globular or fibrous

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

What is a globular protein?

A
  • ball shaped
  • water soluble - hydrophobic turn inwards and hydrophilic outwards
  • have metabolic roles
  • enzymes in all organisms
  • plasma proteins and antibodies in mammals
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What are fibrous proteins?

A
  • form fibres
  • have regular or repetitive sequence of amino acids
  • usually insoluble in water
  • structural roles
  • collagen in bonds and cartilage
  • keratin in fingernails and hair
17
Q

How do you test for proteins?

A

biuret test
- add a few drops of sodium hydroxide solution to sample in test tube (must be alkaline)
- add copper sulphate solution and mix gently
- protein present = turns purples
- no protein = stays blue