Fish fast skeletal muscle tropomyosins show species-specific thermal stability

Ming Chih Huang, Yoshihiro Ochiai

Research output: Contribution to journalArticlepeer-review

42 Citations (Scopus)


Tropomyosin (TM) was isolated from the fast skeletal muscle of six fish species, whose amino acid sequences of this protein have already been revealed. The thermal stability of these TMs was measured by differential scanning calorimetry (DSC) and circular dichroism (CD), while the molecular weights were measured by mass spectrometry. The results showed clear differences in thermostability among these fish TMs, though the identity of amino acid sequences was more than 93.3%. Therefore, only a few amino acid substitutions could affect the overall stability of the TM molecule. Especially, several residues located on the molecular surface were considered to be responsible for such stability difference. In contrast, the molecular weights of these TMs as measured by mass spectrometry were higher than those calculated from amino acid composition, suggesting the presence of post-translational modification(s) which could also affect their thermal stability.

Original languageEnglish
Pages (from-to)461-471
Number of pages11
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Issue number4
Publication statusPublished - 2005 Aug
Externally publishedYes


  • CD spectrum
  • Coiled-coil
  • Differential scanning calorimetry
  • Fish
  • Primary structure
  • Skeletal muscle
  • Thermal stability
  • Tropomyosin
  • α-Helix

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology


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