Ausio J, Toumadje A, McParland R, Becker R R, Johnson W C, van Holde K E
Biochemistry. 1987 Feb 24;26(4):975-82. doi: 10.1021/bi00378a001.
Trypsin digestion of the protamine-like protein from Spisula solidissima has revealed the existence of an internal resistant core. The peptide contains 75 amino acid residues, and its primary structure shows some conserved sequences that are common to those found in the core of the somatic histone H5 from chicken erythrocytes. The secondary structure of this core exhibits 33% antiparallel beta-sheet, 18% beta-turns, 37% random coil, and only 10% alpha-helix, in contrast to histone H5. Hydrodynamic measurements indicate a compact globular assembly for the tertiary structure of this peptide, when compared to the more extended shape observed for the whole protein. The possible relatedness of this protein to the histone H1 family is discussed.
对硬壳蛤中类鱼精蛋白进行胰蛋白酶消化后发现存在一个内部抗性核心。该肽含有75个氨基酸残基，其一级结构显示出一些保守序列，这些序列与鸡红细胞体组蛋白H5核心中的序列相同。与组蛋白H5相比，该核心的二级结构表现为33%的反平行β-折叠、18%的β-转角、37%的无规卷曲，只有10%的α-螺旋。流体动力学测量表明，与观察到的整个蛋白质更伸展的形状相比，该肽的三级结构呈紧密的球状组装。本文讨论了这种蛋白质与组蛋白H1家族可能的相关性。
