Proteins 1&2 Flashcards

(46 cards)

1
Q

Aliphatic amino acids

A

Alkane/organic

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

Basic amino acid

A

Alkaline

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

Aromatic amino acids

A

Benzene

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

Other amino acid

A

Proline

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

Peptide bond

A

Formation of covalent bond with loss of water

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 polypeptide

Versatility in protein structure and function

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

Secondary structure

A

Spatial arrangement of amino acid residues near each other in linear sequence

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

Alpha helix

A

Held in place by hydrogen bonds

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

Beta pleated sheets

A

Hydrogen bonds between amide groups of linear polypeptide chain - porin

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

Tertiary structure

A

Spatial arrangement of amino acid residues that are far apart in a linear sequence

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

Examples of tertiary structure

A

hydrophobic interactions
Disulphide bridges
Van der waals
Hydrogen bonds

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

Ionic interactions

A

2 close oppositely charged R groups strong but rare

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

Van der waals

A

Non specific weak

Stabilise structure as strong together

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

Hydrogen bonds

A

Strong and permanent

1/20 strength of hydrogen bonds

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

Hydrophobic interactions

A

Intra polypeptide

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

Disulphide bridges

A

2 cysteine residues

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

Quaternary structure

A

Spatial arrangement of individual polypeptide chains in a multi sub-unit protein
CRP - high when infected and haemoglobin

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

Denaturation - causes

A

Acids, heats, solvents, cross link reagents, chaotropic agents - molecule in water which disrupts bonds, disulphide bond reducers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

What structures are effected by denaturation?

A

Secondary and tertiary

20
Q

What are the effects of denaturation

A
  • decreased solubility
  • loss of water binding capacity
  • Loss of biological activity
  • Improved digestibility
21
Q

Peptidases

A

Cleave peptide bonds

22
Q

Endopeptidase

A

Cleave internal bonds

23
Q

Exopeptidase

A

Cleave one amino acid at a time

24
Q

Carboxypeptidase

A

Cleave at COOH

25
Aminopeptidase
Cleave at NH2
26
What is protein structure dependent on?
DNA sequence
27
Name 3 other types of proteins
- glycoprotein - Lipoproteins - metalloprotein
28
Glycoprotein
Protein and carbohydrate post translational modification Sugar binds to amino acid
29
Example of glycoprotein
Antibody
30
Roles of glycoproteins
cell recognition and signalling Protein stabilisation solubility
31
Lipoprotein example
LDL, HDL
32
Roles of lipoprotein
Transport water insoluble fats around the body
33
Metalloprotein
1/3 of proteins - metal ion needed for activity
34
Functions of metalloprotein
Transport Enzyme Storage Signalling
35
Globular proteins
Varied function including enzymes, hormones
36
Fibrous proteins
Structural function eg tendon, connective tissue
37
Membrane proteins
Cell/organelle proteins | Transporters and cell adhesion
38
Co-operative binding
Binding at one subunit causes a change in shape of other subunits altering affinity for substrate
39
Scurvy
Amino acid==>hydroxyamino acids Weaker collagen Acquired condition
40
Osteogenesis imperfecta
Small glycine substituted for larger amino acid Not as tight coil, reduced fibril interaction Loss of secondary and tertiary structure Weak and brittle collagen
41
What is the main part of LDL
ApoB
42
What internalises LDL?
Glycoprotein
43
Where is LDL broken down?
Lysosomes
44
Classes of effects and mutations in receptor
- No receptor produced - Receptors never reach cell surface - Receptors cant bind LDL - Receptors don't internalise on binding LDL - Receptors do not release LDL
45
FH
Autosomal dominant | Mutation in LDL receptor
46
Cryoglobulin
Proteins that precipitate in blood and solidify below 37 degrees which is a problem in extremities on a cold day