Protein Separation Flashcards

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

Methods of protein separation

A

1) Differential Solubility
2) Adsorption
3) Size
4) Eletrophoresis

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

Hydration Properties of Proteins

A

+ Water-holding capacity
+ Viscosity modifiers
+ Solubility

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

Protein-Protein Interactions

A

+ Gel formation
+ Precipitation

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

Surface Properties

A

+ Emulsifiers
+ Foaming
+ Surface Tension

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

Biochemical differences of proteins

A

+ Solubility
+ Size
+ Net Charge
+ Adsorption Character.
+ Affinity for other molecules

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

Separation by Differential Solubility

A

1) Salting Out
2) Isoelectric Point Precipitation
3) Solvent Fractionation
4) Denaturation of Other Proteins

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

Salting Out

A

proteins dissolve in water depends on the amount of hydrophilic amino acids present in that particular protein

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

No salt in solution

A

water molecules interact with the charged/hydrophilic amino acids of the protein

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

High Salt Concentration

A

Charged ion interact with water; Proteins molecule aggregate causing precipitation

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

Isoelectric Point

A

the pH at which a protein has no net charge in a solution

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

pH below pI

A

net charge is positive

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

pI is 0

A

less soluble

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

pH is above pI

A

net charge is negative

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

Proteins aggregate and precipitate at their pI because there is

A

no electrostatic repulsion

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

Solvent Fractionation

A

Proteins can be separated based on solubility differences in solvents or solvent mixtures

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

Albumins

A

water soluble

16
Q

Globulins

A

salt soluble

17
Q

Glutelins

A

Soluble in alkali

18
Q

Prolamins

A

soluble in alcohol

19
Q

Water + miscible organic solvents

A

lowers the dielectric constant of water

20
Q

Many proteins are denatured and precipitated from solution when

A

+ Heated above a certain temp

+ Adjusted to highly acid or basic pHs

21
Q

Denaturation

A

change in the conformation of protein
(causing unfolding of a protein)

22
Q

Causes of unfolding (denaturation)

A

+ pH
+ Heat
+ Chemicals (ex. salt)
+ Mechanical Shear (whisking)