sickel cell anemia, ☆MCAD deficiency
usual acidic(negatively chrged) glutamic acid residue is replaced by a nonpolar(neutral charge) valine residue, forming HbS
this leads to the formation of a ☆hydrophobic pocket on the beta globin surface that interacts with a complementary nonpolar residue on another hemoglobin molecule→
this causes polymerization of HbS molecules and subsequent erythrocyte sickling
in HbC disease, glu is replaced by a polar lysine residue, and no hydrophobic interaction
genetics
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