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Stabilization of Deoxy-Hemoglobin by BPG: Mechanisms and Implications

BPG (2,3-bisphosphoglycerate) binds within the cavity formed by the β-chains of hemoglobin, enhancing electrostatic interactions. It specifically stabilizes the deoxygenated (deoxy) form of hemoglobin and cannot bind to its oxygenated (oxy) form. This binding lowers hemoglobin's affinity for oxygen, promoting the release of oxygen to tissues. The interaction between BPG and deoxy-Hb elucidates the critical role of allosteric regulators in oxygen transport dynamics.

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Stabilization of Deoxy-Hemoglobin by BPG: Mechanisms and Implications

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  1. BPG binds in the cavity between the -chains, making electrostatic interactions BPG cannot bind to the oxy form, thus functions by stabilizing the deoxy form. The decrease in oxygen affinity is explained by stabilization of deoxy-Hb

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