Chinese Journal of Magnetic Resonance ›› 1991, Vol. 8 ›› Issue (4): 425-431.

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NMR STUDY OF SILK PROTEIN Ⅲ. High Resolution 13C NMR Studies of Antheraea yamamai

Ji Tao1, Han Xiuwen1, Hu Jiehan1, Zhang Xiaodong2, Yang Nianhua2, Qiu Jiangqing2   

  1. 1. Dalian Institute of Chemical Physics, the Chinese Academy of Sciences;
    2. Wuhan Institute of Physics, the Chinese Academy of Sciences
  • Received:1990-06-19 Revised:1991-01-28 Published:1991-12-05 Online:2018-01-20

Abstract: The 13C CP MAS NMR spectra of three cocoon shells (inside, middle and outside layer of the shell) of Dong Bei Antheraea yamamai (A. yamamai) and Rhodinia fugax were recorded and spectral lines were assigned. The ratioes of main Ine in the spectral area and amorphous region percentage were calculated. The spectra show that the structure of silk protein of Dong Bei Antheraea yamamai cocoon shell is different from that of Rhodinia fugax.

Key words: Antheraea yamamai cocoon shell, Rhodinia fugax, 13C CP MAS NMR spectra