Lecture 8 - Cooperativity and allostery Flashcards

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
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2
Q

The number of ligands bound per site is called the

A

fractional saturation (ϴ)

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3
Q

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

A

sigmoidal

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4
Q

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

A

hyperbolic

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5
Q

Cooperative binding

A

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

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6
Q

Cooperative binding is a property of _______ proteins

A

multisubunit

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7
Q

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

A

increase

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8
Q

Cooperativity is the key mechanism for

A

allosteric regulation

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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

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10
Q

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

A

conformational change

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11
Q

Allosteric activators are

A

effectors that enhance the protein’s activity

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12
Q

Allosteric inhibitors

A

effectors that decrease the protein’s activity

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13
Q

The approach to saturation is controlled only by the

A

binding constant K

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14
Q

Hemoglobin role

A

transport O2 from lungs to tissues

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15
Q

Myoglobin role

A

O2 storage protein

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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

A

T and R

25
Q

In the symmetry model, the ligand can bind to

A

both the T and R states

26
Q

In the symmetry model, the molecular symmetry of the protein must be

A

conserved during conformational changes

27
Q

In the symmetry model, no oligomers contain both

A

T and R states

28
Q

The ______ model allows for a more flexible interaction between a ligand and protein than the symmetry model does.

A

induced-fit

29
Q

The sequential model of cooperativity is based on the

A

induced-fit model

30
Q

The two states, T and R, stand for what?

A

tense (or taught), and relaxed

31
Q

In the sequential model, when a subunit binds oxygen, that subunit changes from the

A

T state to the R state

32
Q

In the sequential model, oligomers can contain

A

both T and R states

33
Q

In the sequential model, the most likely states are

A

the totally empty and the fully bound states

34
Q

In positive cooperativity, the binding of a ligand to one subunit

A

increases the ligand affinity of another subunit

35
Q

In negative cooperativity, the binding of a ligand (inhibitor) to one subunit

A

decreases the ligand affinity of another subunit

36
Q

The essence of the sequential model is that the protein’s ligand binding affinity

A

varies with the number of bound ligands