Lecture 2.1: Intro to Soluble Transport Proteins Flashcards

1
Q

Many of protein functions involve binding

Binding occurs between?

A
  1. Enzymes & their substrates
  2. receptors & signal molecules
  3. transporters & small molecules (for transport)
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2
Q

A ligand is a

A

small molecule that forms a complex with a protein to serve a biological function

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3
Q

The binding of ligands to proteins occurs by [—] interactions

A

weak non-covalent interactions

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4
Q

ligand binding is a [—] association

A

Reversible

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5
Q

Ka

A

association constant/ equilibrium constant for the association (or binding of the protein and ligand)

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6
Q

Keq = Ka

A

[products]/[reactants] = [protein-ligand complex]/[protein][ligand]

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7
Q

Large Ka = [—]

A

high binding affinity

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8
Q

Small Ka = [—]

A

low binding affinity

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9
Q

Kd

A

dissociation constant/ equilibrium constant for the dissociation of ligand from protein-ligand complex

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10
Q

Keq = Kd

A

[reactants]/[products] = [protein][ligand]/[protein-ligand complex]

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11
Q

Large Kd = [–]

A

low binding affinity

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12
Q

small Kd = [–]

A

high binding affinity

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13
Q

fractional saturation

A

the fraction of protein binding sites that are occupied

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14
Q

fractional saturation equation

A

theta =(occupied binding site)/(total binding sites)=[PL]/([PL]+[P])=[L]/([L]+Kd )

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15
Q

Order of Protein Dissociation Constants from Low to High

Biotin-advin
Enzyme-substrate
Typical receptor-ligand interactions
Sequence-specific protein-DNA
Antibody-antigen

A

[High Affinity]
1. Biotin-avidin
2. Antibody-antigen
3. Sequence-specific protein-DNA
4. Typical receptor-ligand interactions
5. Enzyme-substrate
[Low Affinity]

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16
Q

Myoglobin has very [–] Kd for O2 binding

A

low Kd
high binding affinity

17
Q

Myoglobin facilitates oxygen diffusion in [–]

A

muscles

18
Q

Myoglobin structure

A

tertiary
single polypeptide globin
1 heme
MW ~17 kDa
8 alpha helices (75% alpha helices)

19
Q

hemoglobin facilitates oxygen diffusion in [–]

A

red blood cells

20
Q

hemoglobin structure

A

quaternary
4 globin chains (tetramer)
2 alpha and 2 beta subunits
alpha and beta subunits associate to form alpha-beta dimers

21
Q

What type of group is heme?

A

prosthetic group

22
Q

what is a prosthetic group?

A

A non-protein molecule which is permanently attached to a protein and is required for protein function

tightly bound, specific non-polypeptide unit

23
Q

What state must iron be in to bind to O2

A

Fe2+

24
Q

Each heme group can bind [–] ligand

A

one (O2, CO2, CO)

25
Q

Two critical histidine residues and their functions

A

Distal His = stabilizes the O2
Proximal His = forms the other coordinate bond

26
Q

Steps of O2 binding

A
  1. Distal His stabilizes the O2 with H-bonds
  2. oxygen bonds to the heme Fe2+ with one coordinate bond
  3. proximal his forms the other coordinate bond