Location and bond type of intermolecular contacts in the polymerisation of haemoglobin S.
The solubility of 14 hybrid haemoglobins composed of alpha chains with a single substitution and beta chains from HbS was compared with that of sickle haemoglobin. A substantial reduction in the insolubility of native deoxyhaemoglobin S results from surface mutations in certain regions of the alpha chain while changes in other areas have no effect. Also, the chemical nature of the substitution is decisive an points to the type of intermolecular bonding at several loci.
D006451:Hemoglobin, Sickle / Q000235:genetics; D006455:Hemoglobins, Abnormal / Q000235:genetics; D006801:Humans; D006824:Hybridization, Genetic; D009154:Mutation; D010108:Oxyhemoglobins; D010710:Phosphates; D011487:Protein Conformation; D012995:Solubility
D006451:Hemoglobin, Sickle; D006455:Hemoglobins, Abnormal; D010108:Oxyhemoglobins; D010710:Phosphates