lecture 15 biochem

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15 Terms

1
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What is the structure of myoglobin?

Monomeric protein with a single polypeptide chain.

2
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Describe the oxygen-binding curve of myoglobin.

It follows a hyperbolic curve, indicating non-cooperative binding.

3
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How many heme groups are present in hemoglobin?

Hemoglobin contains four heme groups, one in each subunit.

4
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What is the primary function of myoglobin?

Primarily stores oxygen in muscle tissues.

5
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Define the Bohr Effect in the context of hemoglobin.

Refers to how binding of H+ and CO2 inversely affects the binding of O2.

6
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What triggers the conformational change from T state to R state in hemoglobin?

O2 binding triggers this structural change.

7
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What is the significance of the Kd value for myoglobin?

Kd is referred to as p50, the O2 pressure at which myoglobin is 50% saturated.

8
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How does 2,3-bisphosphoglycerate (BPG) affect hemoglobin's affinity for oxygen?

BPG decreases hemoglobin's affinity for oxygen by stabilizing the T state.

9
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What type of curve does hemoglobin's oxygen-binding exhibit?

A sigmoidal curve, which indicates cooperative binding.

10
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Why is the binding of carbon monoxide (CO) to hemoglobin hazardous?

CO has a much higher affinity for hemoglobin than O2, which reduces O2 transport.

11
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What is myoglobin's oxygen-binding affinity compared to hemoglobin?

Myoglobin has a higher oxygen-binding affinity than hemoglobin, as it primarily functions to store oxygen rather than transport it.

12
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In which tissues is myoglobin predominantly found?

Myoglobin is predominantly found in muscle tissues.

13
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What physiological condition can increase the expression of myoglobin?

Physical training or hypoxia can increase the expression of myoglobin in muscles.

14
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How many subunits are present in hemoglobin?

Hemoglobin consists of four subunits, specifically two alpha and two beta chains.

15
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What role does iron play in myoglobin and hemoglobin?

Iron in the heme group of both proteins is crucial for oxygen binding.