Cold adaptation of tropomyosin.

  title={Cold adaptation of tropomyosin.},
  author={Michael Hayley and Tatiana Chevaldina and David H. Heeley},
  volume={50 30},
The conformational stability of unphosphorylated and phosphorylated α,α-striated tropomyosins from rabbit and shark (95% identical sequences) has been investigated. Three additional core positions are occupied by atypical amino acids in the protein from shark: Thr179(d), Ser190(a), and Ser211(a). These changes are thought to have further destabilized most, if not all, of the carboxyl-terminal half of the molecule. Heat-induced unfolding of shark tropomyosin (2 mg/mL, 0.1 M salt, pH 7) as… CONTINUE READING
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