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- NAKAUCHI Yuni
- Department of Biology, Faculty of Science, Chiba University Department of Biology, Faculty of Science, Yamagata University
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- TOYAMA Akira
- Pharmaceutical Institute, Tohoku University
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- MARUYAMA Koscak
- Department of Biology, Faculty of Science, Chiba University Department of Biology, Faculty of Science, Yamagata University
この論文をさがす
抄録
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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- Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences
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Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences 69 (8), 224-226, 1993
日本学士院
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詳細情報 詳細情報について
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- CRID
- 1390282679124420608
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- NII論文ID
- 130000907789
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- NII書誌ID
- AA00785485
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- COI
- 1:CAS:528:DyaK2cXhvVGlu7g%3D
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- ISSN
- 13492896
- 03862208
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- 本文言語コード
- en
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- データソース種別
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- JaLC
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- 抄録ライセンスフラグ
- 使用不可