BCH210H1 Lecture 10: Application of Chou-Fasman Rules to Hemoglobin and the Peptide Hormone Glucagon- Hemoglobin S
31 Dec 2018
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Hemoglobin s: hbs tends to aggregate and forms long fibers, which deform erythrocytes, there is a hydrophobic patch on deoxyhemoglobin s that has a complementary binding site on another deoxyhemoglobin s molecule. Hemoglobin s aggregates via surface hydrophobic interactions: the deoxy forms of hemoglobin s can attach hydrophobic patch to a hydrophobic cleft and that forms a long polymer of aggregated hbs. Space-filling model of a multi-subunit protein hemoglobin: oxygen-bound and non-oxygen bound has different conformations, surface is water soluble (has to travel through plasma of blood) Why does hbs aggregate: renaturation experiments (anfinsen) have shown that information for folding into secondary and tertiary structure is. Coded in the amino acid sequence: combined knowledge of sequence/structure and prediction can provide insight into why hbs is a disease-causing form. Polar mutations cause human diseases: soluble protein, hemoglobin, mutation, domain, disease aqueous sickle-cell anemia. Val664 to glu membrane glioblastoma: membrane protein.
