Murayama M
Science. 1966 Jul 8;153(3732):145-9. 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.
镰状细胞血红蛋白分子的精确比例模型表明，两条β链第6位的谷氨酸被缬氨酸遗传替代，使得分子内形成疏水键。这改变了构象，从而允许分子堆积。旋光色散研究以及将Hb S溶液置于温度变化和丙烷环境中的结果与这种键的存在一致。在磁场和偏振光下对镰状红细胞的检查表明，Hb S分子在原位排列。通过电子显微镜已证实，细丝被解释为由六根Hb S单丝组成的空心缆线。
