Molecular Mechanism of Red Cell "Sickling"

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Science  08 Jul 1966:
Vol. 153, Issue 3732, pp. 145-149
DOI: 10.1126/science.153.3732.145


Precision scale models of sickle-cell hemoglobin molecules indicate that the genetic substitution of valine for glutamic acid at the 6th position in the two beta chains allows an intramolecular hydrophobic bond to form. This changes the conformation in such a way as to allow molecular stacking. Optical rotatory dispersion studies and the restilts of suLbjection of Hb S solution to temperature change and to propane are consistent with the presence of such a bond. Examination of sickled erythrocytes in a magnetic field and in polarized light indicates that the Hb S molecules are aligned iiz sitil. Filaments interpreted as hollow cables of six Hb S monofilaments have been demonstrated by electron microscopy.