Infrared Dichroism of an Elastic Portion (1200kDa Fragment) of Connectin.

  • NAKAUCHI Yuni
    Department of Biology, Faculty of Science, Chiba University Department of Biology, Faculty of Science, Yamagata University
  • TOYAMA Akira
    Pharmaceutical Institute, Tohoku University
  • MARUYAMA Koscak
    Department of Biology, Faculty of Science, Chiba University Department of Biology, Faculty of Science, Yamagata University

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Infrared spectra of an oriented fiber made from 1200 kDa fragment of rabbit skeletal muscle connectin (titin) showed an abundance of β-sheet structures. Infrared dichroism revealed that the β-sheets were alligned with their mainchain axes parallel to the fibre axis. This conclusion is in good agreement with the results of chicken breast muscle β-connectin (Uchida, K. et al., FEBS Lett., 295, 35-38 (1991)). A model of molecular structure of connectin is presented.

収録刊行物

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