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Location and bond type of intermolecular contacts in the polymerisation of haemoglobin S

Nature volume 269, pages 772–775 (1977)Cite this article

Abstract

The solubility of 14 hybrid haemoglobins composed of α chains with a single substitution and β 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 α chain while changes in other areas have no effect. Also, the chemical nature of the substitution is decisive and points to the type of intermolecular bonding at several loci.

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Authors and Affiliations

  1. Department of Biochemistry, College of Physicians and Surgeons, Columbia University, New York, New York, 10032

    Ruth E. Benesch, Suzanna Kwong, Reinhold Benesch & Rohinton Edalji

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  1. Ruth E. Benesch
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  2. Suzanna Kwong
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  3. Reinhold Benesch
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  4. Rohinton Edalji
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Benesch, R., Kwong, S., Benesch, R. et al. Location and bond type of intermolecular contacts in the polymerisation of haemoglobin S. Nature 269, 772–775 (1977). https://doi.org/10.1038/269772a0

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