In healthy patients, the amino acid located at position 6 in the same two protein chains of normal hemoglobin does not interact with phenylalanine 85 and leucine 88 in another hemoglobin protein. Why?
In healthy pateints, the amino acid at position 6 is glutamic acid that is negatively-charged. It does not interact with the phenylalanine 85 and leucine 88 in another hemoglobin protein chain because phenylalanine and leucine are hydrophobic amino acid. Glutamic acid cannot interact with these amino acids as they don't have any charge.
In sickle cell disease, the sixth amino acid in the beta chain that is glutamic acid is replaced by amino acid valine. Valine forms ahydrophobic bond with the phenylalanine 85 and leucine 88 in another hemoglobin protein which distorts the hemoglobin structure by non-covalent polymerisation and becomes sickle-shaped and decreases their elasticity.
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