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Hemoglobin: Difference between revisions
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→Binding of ligands
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When the carbon dioxide levels in the blood increase, hemoglobin can bind protons and carbon dioxide, which causes change in the protein and expedites the release of oxygen. Protons bind a various places with the protein. Also, forming carbamate, carbon dioxide binds at the alpha-amino group. On the other hand, when the carbon dioxide levels in the blood decrease, carbon dioxide is released, increasing the oxygen affinity of the protein. This control of hemoglobin's affinity for oxygen is known as the Bohr effect. | When the carbon dioxide levels in the blood increase, hemoglobin can bind protons and carbon dioxide, which causes change in the protein and expedites the release of oxygen. Protons bind a various places with the protein. Also, forming carbamate, carbon dioxide binds at the alpha-amino group. On the other hand, when the carbon dioxide levels in the blood decrease, carbon dioxide is released, increasing the oxygen affinity of the protein. This control of hemoglobin's affinity for oxygen is known as the Bohr effect. | ||
Molecules, like 2,3-diphosphoglycerate, which lower the affinity of hemoglobin for oxygen, affects the binding of oxygen. When one is accustomed to high altitudes, the concentration of 2,3-diphosphoglycerate in the blood is increase. This allows one to deliver a larger amount of oxygen to each part of tissues that have lower oxygen tension. This phenomenon is called a heterotropic allosteric effect. | Molecules, like 2,3-diphosphoglycerate, which lower the affinity of hemoglobin for oxygen, affects the binding of oxygen. When one is accustomed to high altitudes, the concentration of 2,3-diphosphoglycerate in the blood is increase. This allows one to deliver a larger amount of oxygen to each part of tissues that have lower oxygen tension. This phenomenon is called a heterotropic allosteric effect. <ref name=know/> | ||
== Types == | == Types == | ||
