medium · MCAT bio-biochem
In sickle cell disease, a single missense mutation results in the substitution of a hydrophobic Valine for a hydrophilic Glutamate on the surface of the hemoglobin molecule.
Why does this cause the hemoglobin to polymerize into fibers under low-oxygen conditions?
- The mutation creates new disulfide bridges between hemoglobin subunits.
- The loss of the negative charge on Glutamate prevents the molecules from repelling each other.
- The Valine residue catalyzes a covalent cross-linking reaction.
- The hydrophobic Valine associates with other hydrophobic patches on adjacent molecules.
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