Tenecin 3 : A antifungal active protein with random coil conformation

  • Lee, Young-Tae (Department of Chemistry, School of Natural Science, Korea Advanced Institute of Science and Technology) ;
  • Choi, Byong-Seok (Department of Chemistry, School of Natural Science, Korea Advanced Institute of Science and Technology)
  • Published : 1997.07.01

Abstract

The conformation studies of tenecin 3, which has been purified from the hemolymph of the meal worms Tenebrio molitor, was carried out by CD and NMR. This highly Gly-rich protein consisting of 78 amino acid residues shows similar biochemical features such as heat stability, humoral existence, and high contents of Gly and His residues to other insect antifungal proteins. (omitted)

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