Conformation of the propeptide domain of factor IX

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

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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
Volume1245
Issue number2
DOIs
Publication statusPublished - 1995 Oct 19

Fingerprint

Factor IX
Conformations
Trifluoroethanol
Hemophilia B
Peptides
Blood Coagulation
Point Mutation
Blood Proteins
Blood
Nuclear magnetic resonance
Mutation
Proteins
factor IX Cambridge
Proton Magnetic Resonance Spectroscopy

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Conformation of the propeptide domain of factor IX. / Cheng, Jya Wei; Chen, Chinpan; Huang, Tai Huang; Chou, Shan Ho; Chen, Shi Han.

In: BBA - General Subjects, Vol. 1245, No. 2, 19.10.1995, p. 227-231.

Research output: Contribution to journalArticle

Cheng, Jya Wei ; Chen, Chinpan ; Huang, Tai Huang ; Chou, Shan Ho ; Chen, Shi Han. / Conformation of the propeptide domain of factor IX. In: BBA - General Subjects. 1995 ; Vol. 1245, No. 2. pp. 227-231.
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