Hemoglobin: Difference between revisions

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== Binding of ligands ==
== Binding of ligands ==
With the binding of hemogloin for oxyen, the binding of oxygen is a cooperative process in the tetrameric form of normal adult hemoglobin. Therefore, unlike the normal hyperbolic curve, the oxygen binding curve of hemoglobin is sigmoidal, or 'S' shaped.  
Besides the binding of hemogloin for oxyen, the binding of oxygen is also an essential process in the tetrameric form of normal adult hemoglobin. Unlike the normal hyperbolic curve, the oxygen binding curve of hemoglobin is sigmoidal, or 'S' shaped.  


However, when carbon dioxide is presented and it is at lower pH, Hemoglobin's affinity for oxygen is decreased. To give bicarbonate, Carbon dioxide reacts with water via the reaction:  
However, when carbon dioxide is present and it is at a lower pH level, Hemoglobin's connection to oxygen is decreasing. To get bicarbonate, Carbon dioxide needs to react with water through the reaction:  


* CO<sub>2</sub> + H<sub>2</sub>O {{equilibrium}} HCO<sub>3</sub><small>-</small> + H<small>+</small>  
* CO<sub>2</sub> + H<sub>2</sub>O {{equilibrium}} HCO<sub>3</sub><small>-</small> + H<small>+</small>  


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 combine protons and carbon dioxide, which causes change in the protein and helps to release oxygen. Protons bind a various places with the protein. Also, to form 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's connection level of the protein. This, hemoglobin's control of affection of 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. <ref name=know/>
Molecules, like 2,3-diphosphoglycerate, which lower the affection of hemoglobin for oxygen, affect the binding of oxygen. When one is used to live in high altitudes, the concentration of 2,3-diphosphoglycerate in the blood is increasing. This allows one to carry a large amount of oxygen to each part of the organs and tissues that have lower oxygen tension. This process is called a heterotropic allosteric effect. <ref name=know/>


== Types ==
== Types ==
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