Lecture 8 - Cooperativity and allostery Flashcards

(36 cards)

1
Q

If we have a protein with one binding site for a ligand, the number of ligands bound per site depends on

A
  1. Ligand concentration in solution
  2. Binding constant, K
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

The number of ligands bound per site is called the

A

fractional saturation (ϴ)

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

A binding curve for a ligand and a protein with more than one binding site is _______ shape.

A

sigmoidal

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

A binding curve for a ligand and a protein with one binding site is _______ shape.

A

hyperbolic

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

Cooperative binding

A

The binding of one ligand to one site increases its affinity to the next site

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

Cooperative binding is a property of _______ proteins

A

multisubunit

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

For cooperative binding, the first binding step corresponds to a(n) ______ in Gibbs energy

A

increase

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

Cooperativity is the key mechanism for

A

allosteric regulation

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

Allosteric regulation is

A

the regulation of an enzyme or protein by binding an effector molecule to a site other than the enzyme’s active site

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

Allosteric sites allow effectors to bind to the protein, resulting in a

A

conformational change

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

Allosteric activators are

A

effectors that enhance the protein’s activity

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

Allosteric inhibitors

A

effectors that decrease the protein’s activity

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

The approach to saturation is controlled only by the

A

binding constant K

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

Hemoglobin role

A

transport O2 from lungs to tissues

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

Myoglobin role

A

O2 storage protein

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

For Hill equation, n>1 is

A

positively cooperative binding

17
Q

For Hill equations, n<1 is

A

negatively cooperative binding

18
Q

For Hill equations, n=1 is

A

noncooperative binding

19
Q

In positively cooperative binding, once the ligand molecule is bound to the enzyme, its

A

affinity for other ligand molecules increases

20
Q

In negatively cooperative binding, once the ligand is bound to the enzyme, its

A

affinity for other ligand molecules decreases

21
Q

In noncooperative binding, the affinity of the enzyme for a ligand molecule

A

is not dependent on whether or not other ligand molecules are already bound

22
Q

The two models to describe how ligand binding at one site influences ligand-binding affinity at another identical site

A
  1. symmetry model
  2. sequential model
23
Q

Oligomer

A

a polymer whose molecules consist of relatively few repeating units

24
Q

In the symmetry model, protomers can exist in what states

25
In the symmetry model, the ligand can bind to
both the T and R states
26
In the symmetry model, the molecular symmetry of the protein must be
conserved during conformational changes
27
In the symmetry model, no oligomers contain both
T and R states
28
The ______ model allows for a more flexible interaction between a ligand and protein than the symmetry model does.
induced-fit
29
The sequential model of cooperativity is based on the
induced-fit model
30
The two states, T and R, stand for what?
tense (or taught), and relaxed
31
In the sequential model, when a subunit binds oxygen, that subunit changes from the
T state to the R state
32
In the sequential model, oligomers can contain
both T and R states
33
In the sequential model, the most likely states are
the totally empty and the fully bound states
34
In positive cooperativity, the binding of a ligand to one subunit
increases the ligand affinity of another subunit
35
In negative cooperativity, the binding of a ligand (inhibitor) to one subunit
decreases the ligand affinity of another subunit
36
The essence of the sequential model is that the protein's ligand binding affinity
varies with the number of bound ligands