Chapter 5: Protein Function Flashcards

1
Q

What are ligands?

A

Small organic molecules or other macromolecules that bind to a specific region of a protein (binding site) with specific orientation.

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2
Q

What is affinity and selectivity of a ligand-protein complex?

A

Affinity: how tightly the ligand binds to the protein.
Selectivity: how well the protein discriminates between structurally similar ligands.

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3
Q

What is the receptor protein-ligand complex?

A

-Binds to hormones and other signaling molecules.
- Undergo conformational change and activate signaling process within the cell.

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4
Q

What is the immunoglobulin protein-ligand complex?

A
  • Antibodies (bind to antigens).
  • Recognize foreign macromolecules.
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5
Q

What is the lectin protein-ligand complex?

A
  • Binds to ogliosaccharides.
  • Various functions, all involving the highly specific binding of particular carbohydrate groups.
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6
Q

What is the DNA-binding protein-ligand complex?

A
  • Binds to DNA
  • Transcription factors: bind DNA to regulate transcription of genes.
  • May also bind to other ligands to regulate when they can bind to DNA.
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7
Q

What are transport proteins?

A
  • Bind to various ligands.
  • O2 binding proteins (myoglobin, hemoglobin)
  • Membrane transporters.
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8
Q

What is meant by induced fit?

A

When ligand binding is accompanied by conformational change of protein and/or ligand to accommodate tighter binding.

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9
Q

What does a high Ka imply about protein-ligand interactions?

A

A high Ka means a high concentration of the protein-ligand complex with means there’s a high affinity (tight binding).

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10
Q

What is the fractional occupancy (Y)?

A

Y = (# of occupied binding sites) / (total # of binding sites)

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11
Q

What is Kd a measure of?

A

Affinity

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12
Q

What allows proteins and ligands to bind?

A

H-bonds, van der Waals interactions, electrostatic interactions, and the hydrophobic effect.

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13
Q

What are lectins?

A

Proteins that bind specific oligosaccharides.

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14
Q

What is the final electron acceptor in mitochondria during ATP synthesis?

A

O2

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15
Q

What is Heme?

A

Complexes metal with organic ligands to protect metal from oxidation.

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16
Q

What is Myoglobin (Mb)?

A

Globin found in muscle cells of mammals and other vertebrates.

17
Q

What is proximal His and distal His?

A

Proximal His (His 93 or His F8): Closer to Fe than distal His and forms a coordination complex with De.
Distal His (His 64 or His E7)

18
Q

What is the physiological function of Mb?

A

Provides a reservoir of O2 in the muscle.

19
Q

What is Myoglobin most effective for?

A

O2 storage.

20
Q

What is Hemoglobin (Hb)?

A

Hemoglobin is the primary O2 transport protein in animals.
- Found in red blood cells.

21
Q

What is an allosteric protein?

A

The binding of a ligand (modulator - the second ligand) to one binding site affects the affinity of a different binding site for another ligand.

22
Q

What is homotropic regulation?

A

When the modulator and affected ligand are the same.
- O2 is a positive homotropic regulator for Hb binding to O2.

23
Q

What is heterotropic regulation?

A

When the modulator and affected ligand are different.

24
Q

What does the Hill Equation describe?

A

The Hill Equation described the saturation (fractional occupancy) for a multisubunit protein as a function of [L].
- For a protein with n binding sites for ligand, if the ligands bind with infinite cooperativity (either all sites occupied or no sites occupied):
Y = ([L]^n)/(Kd + [L]^n)

25
Q

What is nH?

A

nH is the Hill coefficient.
- nH < n

26
Q

What does it mean when nH = 1, nH > 1, and nH < 1?

A

nH = 1: no cooperativity.
nH > 1: positive cooperativity.
nH < 1: negative cooperativity.

27
Q

What kind of cooperativity does Mb and Hb have?

A

Mb: No cooperativity as there is only one binding site (nH = 1).
Hb: No cooperativity less then 1 kPa or higher than 10 kPa. In between 1-10 kPa, there’s a higher affinity (nH = 3).