BCH210H1 Lecture Notes - Lecture 10: Hemoglobin, Beta Helix, Beta Sheet
2 Oct 2018
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Sickle cell anemia chronic hemolytic disease that is genetically transmitted. Hbs differs from hba by one aa in the beta sheet. A non conservative mutation: glu is polar, charged. Forms long polymers that changes the shape of rbc. Hbs tends to aggregate and forms long fibers which deforms erythrocytes. Has a hydrophobic patch on deoxyhemoglobin s that has a complementary binding site on another deoxyhemoglobin s molecule. Renaturation experiments have shown that info for folding into 2o and 3o structure is coded in the aa sequence. Combined knowledge of sequence/structure and prediction can provide insight into why hbs is a disease-causing form. Glu is a strong __ helix former. Val is a strong __ sheet former. (p (cid:7571) ) = 1. 06 and (p (cid:7572) ) = 0. 99. (p (cid:7571) ) = 0. 96 and (p (cid:7572) ) = 1. 21. This means that substitution give hbs beta sheet potential. Glu val makes can destabilize the n term region of the protein.
