Molecular Interaction pt 2 Flashcards

1
Q

What are the properties that binding sites for proteins have?

A
  1. Affinity
  2. Competition
  3. Saturation
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2
Q

Ligand

A

Any molecule or ion that binds to another molecules

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3
Q

Substrates

A

Ligands that bind to enzymes & membrane transporters

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4
Q

Protein signal molecules & protein transcription factors are ___________

A

Ligands

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5
Q

__________ are selective about the molecules that they bind to

A

Proteins

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6
Q

Specificity

A

The ability of a protein to bind to a certain ligand or group of related ligands

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7
Q

Protein’s binding reaction are ___________

A

Reversible

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8
Q

Affinity

A

The degree to which a protein is attached to a ligand

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9
Q

If a protein has a _______ affinity for a ligand, then the protein is more than likely to bind to that ligand than to a ligand with a _______ affinity for

A

High, low

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10
Q

The notation for protein ligand binding is what?

A

P + L (reversible arrows) PL

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11
Q

Reversible bind reaction goes to a state of equilibrium where they forward & backward reactions are _________

A

Equal

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12
Q

Binding reaction obey __________

A

Law of mass action

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13
Q

Law of mass

A

When a reaction is at equilibrium the ratio of the products to the substrates is always the same & if it’s distributed by adding or removing the protein or ligand then the reaction will shift in the direction to restore it

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14
Q

The dissociation constant indicates ___________

A

affinity

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15
Q

Keq = [PL]/[P][L]

A

= [PL]/[P][L]

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16
Q

In protein binding reaction the equilibrium constant is a quantitative representation of the proteins’s affinity for the ligand where the ________ the affinity for the ligand the larger Keq is

A

Higher

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17
Q

The reciprocal of the equilibrium constant is the ______________

A

Dissociation constant (Kd)

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18
Q

Kd

A

Kd = [P][L]/ [PL]

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19
Q

A __________ Kd means low binding affinity of the protein to a ligand

A

Large

20
Q

A _______ Kd indicates higher affinity of the protein for the ligand

A

Low

21
Q

If a protein bind to several related ligands than can compare their _______ values to see which ligand is more likely to bind to the protein

A
22
Q

The related ligands that compete for the binding sites are called what?

A

Competitors

23
Q

Agonist

A

Competing ligands that mimic each other’s actions (ex. nicotine mimic a neurotransmitter)

24
Q

Isoforms

A

Closely related proteins whose function is similar but affinity for ligands differ

25
Q

Some proteins are inactive when synthesized in the cell where the activation of some proteins require what?

A

Cofactors

26
Q

Cofactors

A

Is an ion or small organic functional group

27
Q

Ionic cofactors are what?

A

Ca2+, Mg2+, & Fe2+

28
Q

Modulator

A

A factor that influences either protein binding or protein activity

29
Q

The two basic mechanism a modulator does is what?

A
  1. The modular changes the proteins’ ability to bind to the ligand or it
  2. The modular changes the protein’s activity or its ability to create a response
30
Q

Chemical modulars

A

Are molecules that bind covantely or noncovalently to proteins & alter their binding ability to their activity

31
Q

Antagonist (inhibitors)

A

Are chemical modulators that bind to a protein & decrease its activity

32
Q

Competitive inhibitors

A

Are reversible antagonist that compete with customary ligand for the binding site

33
Q

The binding of competitive inhibitors is ___________ where increasing the concentration of the customary ligand can displace the competitive inhibitor & decrease the inhibition

A

Reversible

34
Q

Irreversible antagonist

A

Bind tightly to the protein & can’t be displaced by competition

35
Q

______________ & _____________ modulators may be either antagonist or activators

A

Allosteric & covalent bonds

36
Q

Allosteric modulators

A

Bind reversibly to a protein at a regulatory site away from the binding site & by doing so change the shape of the binding site

37
Q

Allosteric inhibitors

A

Are antagonist that decrease the affinity of the binding site for the ligand & inhibit protein activation

38
Q

Allosteric Activators

A

Increase the probability of protein-ligand binding & enhance protein activity

39
Q

Covalent modulators

A

Are atoms or functional groups that bind covalently to proteins & alter the protein’s properties (They can either increase or decrease a protein’s binding ability or activity)

40
Q

Small changes in pH or temp. act as modulators to __________ or ____________ activity

A

Increase or decrease

41
Q

A denatured protein

A

Protein that lost its shape

42
Q

The body regulates the amount of ___________ in the body

A

Proteins

43
Q

Up regulation

A

The production of new proteins such as receptors, enzymes, & membrane transporters

44
Q

Down regulation

A

The removal of proteins

45
Q

Saturation in proteins

A

When a protein is fully occupied & rate reaches its maximum value

46
Q

__________ applies to enzymes, membrane transporters, receptors, binding proteins & immunoglobulins

A

Saturation