Conformation of the propeptide domain of factor IX

Jya Wei Cheng*, Chinpan Chen, Tai Huang Huang, Shan Ho Chou, Shi Han Chen

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


The propeptide domain in the precursor forms of blood clotting proteins contains the recognition sequences for γ-carboxylase. In hemophilia B, several point mutations in this propeptide domain are responsible for the inherited disease. A peptide containing the propeptide sequence of factor IX was synthesized by solid phase methods. Two dimensional 1H-NMR and CD studies indicate that this peptide motif adopts an α-helical structure in a 40% trifluoroethanol-containing aqueous solution. The results suggest that the amphipathic α-helix within the propeptide domain of factor IX could create a recognition surface for γ-carboxylase. The influences of mutations and their relationship with the α-helical structure are discussed.

Original languageEnglish
Pages (from-to)227-231
Number of pages5
JournalBBA - General Subjects
Issue number2
Publication statusPublished - 1995 Oct 19
Externally publishedYes


  • Blood clotting proteins
  • CD
  • Factor IX
  • Hemophilia B
  • NMR
  • Propeptide
  • Solution conformation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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