✦ LIBER ✦

Tertiary structure of sickle cell hemoglobin and its functional significance

✍ Scribed by Makio Murayama

Publisher: John Wiley and Sons
Year: 1966
Tongue: English
Weight: 914 KB
Volume: 67
Category: Article
ISSN: 0021-9541
DOI: 10.1002/jcp.1040670405

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✦ Synopsis

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 p 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 i n situ. Filaments interpreted as hollow cables of six Hb S monofilaments have been demonstrated by electron microscopy.

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