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Biochemistry C785 WGU Module 3. All Latest Revision Questions and Correct Answers 2024 Update. Graded 100%. $7.99   Add to cart

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Biochemistry C785 WGU Module 3. All Latest Revision Questions and Correct Answers 2024 Update. Graded 100%.

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  • Biochemistry
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  • Biochemistry

Biochemistry C785 WGU Module 3. All Latest Revision Questions and Correct Answers 2024 Update. Graded 100%.

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  • October 4, 2024
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  • Biochemistry
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Bio-Chem C785 - WGU - Module 3 – All Questions And
Answers
Carbon monoxide outcompetes oxygen for attachment to the heme group of hemoglobin

where it is permanently, covalently attached. - True.
As carbon monoxide binds to hemoglobin, the protein subunits change conformation to allow

carbon monoxide to bind faster, This process is called - positive cooperatively.
Carbon monoxide shifts the oxygen-hemoglobin dissociation curve to the left, while carbon
dioxide shifts this curve to the right. Based on your knowledge of the Bohr Effect, what is

true? - Carbon dioxide decreases the hemoglobin's affinity for oxygen, while carbon
monoxide increases it.
Hemoglobin's cooperative binding behavior is key to its physiological function, the binding

of which molecules influences this behavior? - Oxygen
Carbonic anhydrase is an important enzyme present in the red blood cells that aids in efficient
transportation of carbon dioxide in the form of bicarbonate ions, from tissues to lungs. -

True
Hemoglobin’s ability to bind or release oxygen depends on the pH of the environment. This
behavior is known as the Bohr Effect, thus Hemoglobin binds to the oxygen at high pH and

releases oxygen at a low pH. - True
Hemoglobin acts as a buffer and controls the pH of the blood by binding to h+ ions. -

True
In the lungs, CO2 concentration is low and the pH is high, while in the tissues, the CO2

concentration is high and the pH is low. - True
In the locations where the pH is low, hemoglobin will be in the T state, allowing it to release

oxygen more effectively - True
Increased levels of 2,3-BPG will decrease the affinity for oxygen by binding to and
stabilizing the T state of hemoglobin. The action of 2,3-BPG allows hemoglobin to release
oxygen more effectively, which is similar to the effect of low pH on the action of

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