Hemoglobin Cooperativity quiz #1 Flashcards
Hemoglobin Cooperativity quiz #1
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What is positive cooperativity in hemoglobin, and how does it affect oxygen binding?
Positive cooperativity in hemoglobin means that the binding of one oxygen molecule increases the affinity of the remaining subunits for oxygen, resulting in a sigmoidal (S-shaped) oxygen binding curve. How does the oxygen binding curve of hemoglobin differ from that of myoglobin, and what does this indicate about their functions?
Hemoglobin has a sigmoidal oxygen binding curve due to cooperativity, while myoglobin has a hyperbolic curve with no cooperativity. This means hemoglobin is better at releasing oxygen to tissues, whereas myoglobin holds onto oxygen tightly. What structural feature of hemoglobin allows it to exhibit cooperativity, unlike myoglobin?
Hemoglobin has multiple subunits (it is a tetramer), which allows for cooperative interactions, while myoglobin is a monomer and cannot exhibit cooperativity. Describe the T (tense) and R (relaxed) states of hemoglobin and their roles in oxygen binding.
The T state (tense) has low affinity for oxygen and predominates at low oxygen levels, while the R state (relaxed) has high affinity for oxygen and is favored as more oxygen binds, facilitating cooperative binding. What are the concerted and sequential models of cooperativity, and how do they apply to hemoglobin?
The concerted model suggests all subunits switch between T and R states simultaneously, while the sequential model proposes subunits change states one at a time. Hemoglobin's behavior is best explained by a combination of both models. Why is partial pressure of oxygen (pO2) used on the x-axis of oxygen binding curves for hemoglobin?
Partial pressure of oxygen (pO2) is used because oxygen is a gas, and its concentration in biological systems is best represented by its partial pressure, which is directly proportional to its concentration. How does hemoglobin's positive cooperativity make it a superior oxygen transporter compared to myoglobin?
Hemoglobin's positive cooperativity allows it to efficiently load oxygen in the lungs and release a large amount in tissues, optimizing oxygen delivery, while myoglobin binds oxygen tightly and releases very little. What is the threshold effect in hemoglobin, and how does it benefit oxygen delivery to tissues?
The threshold effect refers to hemoglobin's ability to release more oxygen in response to lower tissue oxygen levels, ensuring that active tissues receive more oxygen when needed. Explain why myoglobin is not an effective oxygen transporter in the body.
Myoglobin has a very high affinity for oxygen and does not release it efficiently at tissue oxygen levels, making it poor at delivering oxygen to where it is needed. What is a homotrophic allosteric activator, and how does oxygen act as one for hemoglobin?
A homotrophic allosteric activator is a molecule that increases the protein's affinity for itself; oxygen acts as one for hemoglobin by increasing its own binding as more oxygen molecules bind. How do allosteric effectors like BPG influence hemoglobin's oxygen release?
Allosteric effectors like BPG decrease hemoglobin's affinity for oxygen, promoting greater oxygen release to tissues and enhancing hemoglobin's role as an oxygen transporter. Summarize the main reason hemoglobin is more effective than myoglobin at delivering oxygen to tissues.
Hemoglobin's cooperative binding and ability to respond to changes in oxygen demand make it highly effective at delivering oxygen to tissues, unlike myoglobin, which holds onto oxygen too tightly.
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