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- W2023367952 abstract "Precision scale models of sickle cell hemoglobin molecules indicate that the genetic substitution of valine for glutamic acid at the sixth position in the two β chains allows an intramolecular hydrophobic bond to form. This changes the conformation in such a way as to allow molecular stacking. Results of subjection 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 in situ. Filaments interpreted as hollow cables of six Hb S monofilaments have been demonstrated by electron microscopy." @default.
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- W2023367952 title "Tertiary structure of sickle cell hemoglobin and its functional significance" @default.
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