| Abstract: | The tentative elucidation of the 3D-structure of vitellogenesis inhibiting hormone (VIH)
peptides is conversely underprivileged by difficulties in gaining enough peptide or protein,
diffracting crystals, and numerous extra technical aspects. As a result, no structural
information is available for VIH peptide sequences registered in the Genbank. In this
situation, it is not surprising that predictive methods have achieved great interest. Here, in
this study the molt-inhibiting hormone (MIH) of the kuruma prawn (Marsupenaeus
japonicus) is used, to predict the structure of four VIHrelated peptides in the
crustacean species. The high similarity of the 3D-structures and the calculated physiochemical
characteristics of these peptides suggest a common fold for the entire family. |
