Macromolecules and Bichemistry of Sickle Cell Disease

     Sickle Cell Disease is caused by something as small as a shift in amino acids of a protein.  In hemoglobin the substitution of an amino acid called valine  for glutamic acid at a certain spot in the primary structure is what causes Sickle Cell Disease.  This mutation causes the whole protein to denature.  Because of the denaturation the molecules of the hemoglobin crytilize forming fibers that are limited in their ability to carry oxygen in the cell membrane.  This also makes the red blood cells form a sickle shape instead of the normal disk shape of a red blood cell.^[1]

     The first picture below is of normal hemeoglobin.  The four gray spots are noncovalently bonded heme groups.  These are contact sites for one molecule of oxygen.  In the second picture the gray heme groups are small and broken up.  The gray clusters purpose is to bind and help transport oxygen, because they are deformed it impedes the hemoglobins ability to move oxygen.^[2]

      ^[3]

Ally Gatmaitan and Alex Schwent