A synthetic peptide mimics troponin I function in the calcium-dependent regulation of muscle contraction

Jennifer E. Van Eyk, John D. Strauss, Robert S. Hodges, J. Casper Rüegg

Research output: Contribution to journalArticlepeer-review

Abstract

A new technique for treating skinned cardiac muscle fibers has been developed in which troponin I is extracted, giving rise to unregulated fibers. The effect of the 12-residue troponin I peptide on these fibers indicates that this region of troponin I is solely responsible for muscle relaxation (inhibition of force). Furthermore, troponin I peptide-troponin C reconstituted fibers are stable through several contraction-relaxation cycles indicating the peptide can switch binding sites between actin and troponin C. The troponin I peptide can substitute for the native protein as part of the calcium-sensitive molecular switch that controls muscle regulation.

Original languageEnglish (US)
Pages (from-to)223-228
Number of pages6
JournalFEBS Letters
Volume323
Issue number3
DOIs
StatePublished - Jun 1 1993

Keywords

  • Muscle regulation
  • Protein-protein interaction
  • Synthetic peptide
  • Troponin I

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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