Solution structure of trypsin modulating oostatic factor is a left-handed helix

Academic Article

Abstract

  • The solution structure of trypsin modulating oostatic factor (TMOF), a decapeptide (H-YDPAPPPPPP-OH) hormone that signals the termination of trypsin-like biosynthesis in mosquito midgut epithelial cells, was determined by 2-D 1H nuclear magnetic resonance spectroscopy and molecular modeling. The peptide forms a rod-shaped left-handed helix about 30 Å long. No evidence was found to support a poly-L-proline β-turn model. Hydrophobic contacts between the rings of tyrosine 1 and proline 3 may enhance the stability of the N-terminal segment. This peptide provides an interesting exception to the normal chemical shift index (csi) rules. Our results suggest that a sequence of positive csi indices, normally expected for a β-strand structure, could also describe a left-handed poly-L-proline-like helix. © 1993 Academic Press, Inc.
  • Digital Object Identifier (doi)

    Pubmed Id

  • 17405810
  • Author List

  • Curto EV; Jarpe MV; Blalock JE; Borovsky D; Krishna NR
  • Start Page

  • 688
  • End Page

  • 693
  • Volume

  • 193
  • Issue

  • 2