Proteins 2.1.2 (k,l,m,n,o) Flashcards

(43 cards)

1
Q

monomer of a protein?

A

amino acids

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

what is formed with two amino acids?

A

a dipeptide

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

what is an amino acid chain?

A

a polypeptide

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

what bonds link amino acids together?

A

peptide bonds

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

what reaction forms peptide bonds?

A

condensations

a molecule of water is produced

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

what reaction destroys peptide bonds?

A

hydrolysis

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

what are the levels to protein structure?

A

primary
secondary
tertiary
quaternary

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

what is the primary structure of a protein?

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
10
Q

what bonds are present in the primary structure?

A

peptide bonds

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

what is the secondary structure of a protein?

A

the coiling of the polypeptide chain into:
- alpha helix
- beta pleated sheet

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

alpha helix

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

beta-pleated sheet

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

what bonds are present in the secondary structure?

A

peptide bonds
hydrogen bonds

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

what is the tertiary structure of a protein?

A

the further folding of a polypeptide chain into it’s 3D structure

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

what bonds are present in the tertiary structure?

A

ionic
disulfide bridges
hydrophobic-hydrophilic interactions
hydrogen bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

in the tertiary structure what are the bonds formed between?

A

the R-groups of a protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

ionic bonding

A

between oppositely charged R-groups

19
Q

disulfide bridges

A

between two R-groups which both contain cysteine

20
Q

hydrophobic-hydrophilic interactions

A

between hydrophobic and hydrophilic R-groups

21
Q

hydrogen bonds

A

between delta +ve and delta -ve R -groups

22
Q

what is the quarternary structure?

A

the interactions between more than one polypeptide chain

the final 3D structure

23
Q

what are the two types of protein?

A

globular
fibrous

24
Q

properties of globular proteins

A

compact
spherical
water soluble

25
how are globular proteins water soluble?
they have their hydrophobic R-groups pointing inwards they have their hydrophilic R-groups pointing outwards
26
why is water solubility important for globular proteins?
they have to be able to be dissolved in water to be transported
27
examples of globular proteins
insulin haemoglobin catalase
28
role of insulin
hormone which decreases the blood glucose level
29
structure of insulin
two polypeptide chains joined together by disulfide bridges
30
what is a conjugated protein?
a protein which contains a non-protein element called a prosthetic group
31
example of a conjugated protein
haemoglobin
32
what is the prosthetic group in haemoglobin?
Fe2+
33
structure of haemoglobin
4 polypeptides with 2 alpha and 2 beta subunits each subunit contains a prosthetic group of Fe2+
34
what does the Fe2+ do?
binds to oxygen or carbon dioxide which allows haemoglobin to transport it around the body
35
why does haemoglobin have to be water soluble?
it needs to be able to dissolve in the blood to be transported around the body
36
role of catalase
breaks down hydrogen peroxide
37
structure of catalase
four prosthetic groups each have their own haem grou[
38
properties of fibrous proteins
long insoluble strong - high tensile strength
39
properties of fibrous proteins
long insoluble strong - high tensile strength
40
examples of fibrous proteins
collagen keratin elastin
41
properties of collagen
strong flexible insoluble
42
what makes collagen strong?
presence of cysteine means that disulfide bridges are formed which require a lot of energy to overcome
43
properties of elastin
flexible