Premium
Tertiary structure of sickle cell hemoglobin and its functional significance
Author(s) -
Murayama Makio
Publication year - 1966
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040670405
Subject(s) - hemoglobin , molecule , intramolecular force , stacking , crystallography , electron microscope , chemistry , biophysics , stereochemistry , biochemistry , biology , physics , organic chemistry , optics
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.