罗马蜗牛（Helix pomatia）β-血蓝蛋白壁域的重组。

Torensma R, van der Laan J M, Zantinge A G, van Bruggen E F

Biochem J. 1981 Apr 1;195(1):119-22. doi: 10.1042/bj1950119.

beta-Haemocyanin molecules consist of 20 very large polypeptide chains. These chains are composed of eight structural domains. So-called 'collar' domains can be removed by trypsinolysis of the native cylindrical molecule, resulting in an association of the remaining hollow cylinders into large tubular polymers. Dissociation of the tubular polymers gives one single- and four multi-domain fragments. The role of these fragments in the reassembly process of these tubular polymers was investigated. The two-domain fragment could form tubular polymers. The other domain fragments were not able to form tubular polymers unless in the presence of the two-domain fragment. Tubular polymers with enlarged diameter and ribbon-like structures were observed in the reassembly products when the one-domain fragment was omitted.

β-血蓝蛋白分子由20条非常大的多肽链组成。这些链由八个结构域构成。通过对天然圆柱形分子进行胰蛋白酶消化可以去除所谓的“衣领”结构域，从而使剩余的空心圆柱体缔合形成大型管状聚合物。管状聚合物解离后产生一个单结构域片段和四个多结构域片段。研究了这些片段在这些管状聚合物重新组装过程中的作用。双结构域片段能够形成管状聚合物。其他结构域片段除非在双结构域片段存在的情况下，否则无法形成管状聚合物。当省略单结构域片段时，在重新组装产物中观察到了直径增大且呈带状结构的管状聚合物。