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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
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 alpha-helix, in the insoluble conformation the protein is mostly composed of beta-sheets. Dimerization of NT create fiber of spider silk and the changing conformation from alpha-helix to beta-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
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
