Figure 11. This picture shown the assembly structure of the scaffold protein spectrin and its spatial configuration, and were proposed a deformation hypothesis of our model.

(A) The figure was a schematic diagram of spectrin and other cytoskeletal molecules. (B) Stereoview ribbon diagram of the overall structure of spectrin protein in all the repeats around the kink region. The first and second repeat (α, β subunit) were shown in light blue, and the linker region between repeats in purple, Residues were numbered according to the SWISS-PROT NP_003117.2 entry, and the residues from 1 to 2149 aa of Homo sapiens. Lastly, the software of the PyMOL Molecular Graphics Systerm was used to simulate the molecular structure, including a complete of the molecular structure and partial structure were displayed. (C) A series of random deformation process will be shown. The figure was α-spectrin in dark red band, and β-spectrin with a white band, the shape of saw tooth was rupture boundary. C₁ represented for completely without any deformation, then, C₂, C₃ and C₄ respectively shown that from a set of skeleton to three groups of skeleton were broken. But the case of C_N manifested randomly the fracture of cytoskeletal protein. Thus, this phenomenon could reflect the uninterrupted and dynamic of changes from small deformation to large deformation during the radiation, and more details were explained in the article.