BCH210H1 Lecture Notes - Affinity Chromatography, Beta Sheet, Hemoglobin
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BCH210H1 Full Course Notes
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Hemoglobin is a oxygen carrier with 4 subunits. Hemoglobin s differs from hba in one amino acids in the beta chain glu-6 to val-6. This is a non-conservative mutation: glu is a polar charged amino acid, val is a highly non polar amino acid. Hbs is more positive then hba and will be closer to the negative charge in the sds-page. Hbs tends to aggregate and form aggregated fibers which precipitates into clumps. Apparently there is a hydrophobic patch on deoxyhemoglobin s which has a complementary site on another deoxyhemoglobin s molecule (aggregation happens in the deoxy form) Cf p-values show that glu is a higher helix former and val is a higher beta sheet former. Since beta sheets are inter- rather than intra molecular structures cf analysis predicts the. In hba can be either in a helix or beta sheet but in hbs there is increased beta-sheet potential change in protein properties. (aggregating is using inter molecular bonds)
