Hemoglobin 2

The video explores the concept of cooperativity, focusing on hemoglobin's positive cooperativity, where oxygen binding becomes more favorable with each subsequent oxygen molecule. It discusses structural changes in hemoglobin upon oxygen binding, emphasizing the role of histidine. The Bohr effect is explained, showing how pH affects hemoglobin's oxygen saturation. Finally, the video covers allosteric modulation, differentiating between positive and negative modulators.

Explain the relationship between pH and the T state of hemoglobin.

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What happens to hemoglobin's percent saturation with oxygen as pH decreases?

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What are allosteric modulators and how do they affect hemoglobin?

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Differentiate between homotropic and heterotropic allosteric modulators with examples.

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