Function
MaSp1 is one of the proteins which composed the spider silk. The N-terminal domain (NT) is important to change from the soluble conformation of MaSp1 to the insoluble of this protein. In the soluble conformation the most important secondary structure is α-helix, in the insoluble conformation the protein is mostly composed of β-sheets. Dimerization of NT create fiber of spider silk and the changing conformation from α-helix to β-sheets make the spider silk insoluble. The dimerization of NT is induced by the lowering of pH from 7 to 6.
Relevance
Understand the polymerization of spider silks is important to produce this in vitro and in great quantity. Indeed the militaty and biomedical fields need spider silks to develop different product like bullet proof vest, artifical bones and artifical ligament.
Structural highlights
