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Question: Normal hemoglobin’s beta-globin chain has a glutamate (Glu. E) residue at the 6^th position. The …

Question: Normal hemoglobin's beta-globin chain has a glutamate (Glu. E) residue at the 6^th position. The ...

Normal hemoglobin’s beta-globin chain has a glutamate (Glu. E) residue at the 6^th position. The sickle-cell mutation changes this rescue into a valine (Val, V) residue. This is often written as Glu6(beta)Val. This change is sufficient to cause the sickle-cell hemoglobin tetramers to associate with each other and assemble into large fibers that changes the red blooded morphology (shape): Sickle-cell erythrocytes (=red blood cells) assume a stereotypic crescent shape. Such “sickle-cells” are more fragile, leading to their breakage, the loss of the hemoglobin and the anemic presentation of the disease. Normal hemoglobin tetramers, on the other hand, do not associate with each other but rather remain soluble within the erythrocytes that maintain their shape as round biconcave disks that are flattened (depressed) in their center. Such cells are flexible and can easily squeeze through even the narrowest capillaries. What is the difference between the two amino acids and how can it explain the change in the structure of the protein? Glutamate is negatively charged at physiological pH and is repelled by another negatively charged residue on other tetramers, thus it is prevented from interacting with them. On the other hand, valine is positively charged and is therefore attracted to those negatively charged residues, thus forming a long chain of tetramers. Glutamate is negatively charged at physiological pH and interacts well with a positively charged group on another tetramer. However, valine is hydrophobic preventing its interaction with that group and therefore the formation of a chain of tetramers is prevented. Glutamate is hydrophobic and is forced because of the hydrophobic effect to interact with another another tetramer. In turn this tetramer is interacting with yet another tetramer, thus forming a long chain of tetramers. Valine on the other hand is negatively charged at physiological pH and interacts well with the water around it and remain soluble. Glutamate is negatively charged at physiological pH and interacts well with the water around it. However, valine is hydrophobic and is forced because of the hydrophobic effect to interact with another valine on another tetramer. In turn this tetramer is interacting with yet another tetramer, thus forming a long chain of tetramers.

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