Petruzzelli R, Goffredo B M, Barra D, Bossa F, Boffi A, Verzili D, Ascoli F, Chiancone E
FEBS Lett. 1985 May 20;184(2):328-32. doi: 10.1016/0014-5793(85)80632-3.
The dimeric hemoglobin (HbI) from Scapharca inaequivalvis is highly homologous to the other known dimeric Acid hemoglobins. The sequence has a distinctive hydrophobicity profile in the region corresponding to the E and F helices with respect to both the hemoglobin and myoglobin chains from vertebrates due to the presence of several additional hydrophobic residues. The characteristic topology of the E and F helices is conserved in all the known sequences of Arcid hemoglobins including that of the so-called alpha chain of the tetrameric component from Anadara trapezia. The rationale for this conservation lies in the unusual assembly of Arcid hemoglobins where the E and F helices are involved in the interdimeric contact. It is suggested that the extra hydrophobic residues play a major role in the assembly of the basic dimeric unit in these hemoglobins.
不等齿毛蚶的二聚体血红蛋白（HbI）与其他已知的二聚体酸性血红蛋白高度同源。由于存在几个额外的疏水残基，相对于脊椎动物的血红蛋白和肌红蛋白链，该序列在对应于E和F螺旋的区域具有独特的疏水性分布。E和F螺旋的特征拓扑结构在所有已知的蚶科血红蛋白序列中都是保守的，包括梯形蚶四聚体成分所谓的α链的序列。这种保守性的基本原理在于蚶科血红蛋白的特殊组装方式，其中E和F螺旋参与二聚体间的接触。有人认为，额外的疏水残基在这些血红蛋白基本二聚体单元的组装中起主要作用。
