Proteins Flashcards

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

describe the basic structure of an amino acid.

A

carbon, amine group (NH), carboxylic acid group (COOH), varying side chain

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

Name 4 basic categories of amino acids

A

Acid, Basic, Uncharged Polar, Non - Polar

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

Name 2 acidic amino acids.

A

will have carboxylic acid group
Aspartic acid
Glutamic acid

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

Name some basic amino acids

A

Will have NH3.

lysine, arginine, histidine

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

Name some uncharged polar amino acids.

A
Will have OH or something 
Glutamine 
Serine
Threonine 
Tyrosine 
Asparagine
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Name some non - polar amino acids

A

glycine, alanine, methionine, cysteine, valine, proline, phenalynine, tryptonphan, leuchine etc.

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

what is a proteins primary structure?

A

Amino acids joined by peptide bonds. condensation reaction - H20 lost.

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

What is a proteins secondary structure?

A

The spatial arrangement of amino acid residues that are near each other in the linear sequence.

Alpha helixes- H bonds NH group and C=O group of next amino acid.

Beta Sheet. - pleated structure. beta strands (3-10 amino acids) connected by hydrogen bonds

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

What is a proteins tertiary structure?

A

The spatial arrangement of amino acid residues that are far apart in the linear sequence. Due to:
Van der waals
Ionic Interactions (strong bond between opposite charges)
Hydrogen bonding (H - O, N, F)
Disulphide bridges - strong covalent bond
Hydrophobic interactions

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

What is a proteins quartanery structure?

A

Multisubunit protein, e.g haemoglobin.

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

What is meant by protein denaturing?

A

Disruption / destruction of secondary and tertiary structure by things such as heat, solvent, acid etc.

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

How can denaturation effect a protein?

A

Could effect solubility
Loose activity
Improve digestibility etc.

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

What are glycoproteins? give an example.

A

e.g immunoglobins
Protein +carb
Formed by glycolysation
(can look to detect diabetes)

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

what is a lipoprotein?

A

Protein and lipid. Transports insoluble fat and cholesterol in blood

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

What are metalloproteins?

A

proteins and metal - 1/3 of proteins require metal to work.

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

Haemoglobin has co-operative binding. What does this mean?

A

When haeme in one subunit binds to a molecule of O2, the other’s affinity for O2 will increase.

17
Q

How is sickle -cell anaemia caused and what is it?

A

single point mutation.

Red blood cells become dodgy, give up O2 easily, insoluble, clump together

18
Q

How can u figure out what proteins someone has

A

Serum protein electrophoresis