Chapter 7 Review Flashcards

1
Q

In terrestrial animals, myoglobin…

A
  • Increases O2 solubility

- Promotes O2 diffusion into tissue

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2
Q

In marine animals, myoglobin…

A
  • Promotes O2 diffusion
  • 10x amount of Mb present
  • Functions in O2 storage
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3
Q

Structure of the Sperm Whale myoglobin was discovered by ___________. It was the first _____ of a protein.

A

John Kudrow (1959) ; protein crystallography

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4
Q

Myoglobin is known for two important jobs

A

1) Binding and releasing O2

2) Helps diffuse CO2 throughout the body

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5
Q

Sperm Whale myoglobin is a ___ protein. It has a total of _________. Heme (protoporphyrin 9). Fe(II) is the metal in the middle. Contains ________ and _________.

A

Pyroles and histidine residues

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6
Q

What is the proximal histidine?

A

The histidine attached to the Fe atom

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7
Q

Can Fe (II) convert to Fe (III)?

A

Yes, when Fe(II) becomes Fe(III), this means that an e- is lost. Once Fe (III) is formed, it can’t bind to oxygen and myoglobin is not useful anymore.

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8
Q

The protein _________the heme _______ and non-oxygen things.

A

protects ; from oxidation

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9
Q

Ka is __________ to Kd.

A

inversely proportional

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10
Q

Why do partial pressure values matter?

A

Pressure helps dissolve O2 into the blood.

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11
Q

YO2 = (PO2)/(Kd+pO2)

A

Dalton’s Law of Partial Pressure

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12
Q

YO2 vs. PO2 hyperbolic curve means

A

myoglobin binding

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13
Q

The greater the partial pressure, the ________ the solubility.

A

greater

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14
Q

Fraction bond is equal to _____.

A

Dissociation constant

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15
Q

Lower affinity for oxygen on a myoglobin partial pressure graph will cause the graph to

A

move to the right and become more shallow

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16
Q

The quaternary structure of hemoglobin is ________.

A

heterodimer

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17
Q

Oxygenation of a heme group means

A

oxygen is binding to the heme group

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18
Q

When Fe(II)-heme complex is oxygenated

A
  • The electronic state is altered

- The color changes from dark purple to red.

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19
Q

Define fractional saturation

A

the O2 dissociation of myoglobin. The fraction of O2-binding sites occupied by O2. (Value ranges from 0 ,or no O2 bound, to 1, or all the binding sites of all the myoglobin molecules are occupied)

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20
Q

low pO2 of myoglobin means

A

little O2 binds to the myoglobin

21
Q

high pO2 of myoglobin means

A

virtually all O@_BINDING SITES ARE OCCUPIED> Myoglobin is saturated with O2.

22
Q

As pO2 of myoglobin increases, ______ O2 binds to the myoglobin.

A

more

23
Q

p50

A

the oxygen pressure at which myoglobin is 50% saturated

24
Q

p50 of myoglobin

A

2.8 torr

25
Q

Myoglobin brings oxygen to the ________ of ________ cells.

A

capillaries ; muscle

26
Q

Hemoglobin is a _____. It has ____ C2 symmetry and ____ symmetry.

A

α2β2 tetramer ; exact ; pseudo-D symmetry

27
Q

Hemoglobin has a _______ quaternary structure.

A

heterodimer

28
Q

Hemoglobin is made of _____ subunits: 2 _ and 2 _

A

4 ; α ; β

29
Q

When oxygen binds to hemoglobin, the ______ of hemoglobin changes.

A

structure

30
Q

T-State

A

Deoxy hemoglobin, low affinity for oxygen

31
Q

R-State

A

Oxy hemoglobin, high affinity for oxygen

32
Q

_____ degree rotation causes R-state to go back to T-state.

A

15

33
Q

Hemoglobin partial pressure curve is ______.

A

Sigmoidal

34
Q

Define cooperativity.

A
  • The proteins “work” together.
35
Q

Define allosteric effect

A

A small molecule whose binding to a protein affects the function of another site on the protein.

36
Q

In hemoglobin, _____ prevents the release of oxygen.

A

cooperativity

37
Q

____________ transports the oxygen from the hemoglobin to the cell.

A

myoglobin

38
Q

What prevents veins busting from the built up pressure from CO2 when exercising?

A

carbonic anhydrase promotes the forward reaction of CO2 + H2O H+ + HCO3-

39
Q

At higher pH, hemoglobin _______ its oxygen

A

releases

40
Q

What is Allostery?

A

Communication between subunits.

41
Q

Symmetry Model of Allosterism

A
  • T-state and R-state are always talking back and forth. They are in the same state.
  • A model of allosteric behavior in which all subunits of an oligomeric protein are constrained to change conformation in a concerted manner so as to maintain the symmetry of the oligomer.
42
Q

Sequential Model of Allosterism

A
  • T-state goes to R-state and reverse.
  • A model of allosteric behavior in which the subunits of an oligomeric protein change conformation in a stepwise manner as the number of bound ligands increases.
43
Q

A normal RBC has Pro-Glu-Glu. A sickle-cell RBC will have the mutation __________.

A

Pro-Val-Glu

44
Q

Vaccines stimulate _____.

A

T-cells

45
Q

Antibody response is part of the _______ immune response.

A

humoral

46
Q

Antibodies (aka immunoglobins) have ________ bonds. ___ C-termini. 2 _____chains and 2 _______ chains.

A

Disulfide bonds ; 4 ; heavy and light

47
Q

Fab

A

“Arms” of the antibody. Antigen binding; variable binding region (antigen coded by hypermutatable region.

48
Q

What is Neutralization in immunology?

A

Antibodies surround the antigen to prevent the virus from binding to the host cell.