STUDIES ON THE FINE STRUCTURE OF SILKFIBROIN

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Other Title
  • 絹フィブロインの微細構造に関する研究
  • キヌ フィブロイン ノ ビサイ コウゾウ ニ カンスル ケンキュウ 3 サクサン フィブロイン ニ オケル アルファ-Helix ノ カクニン
  • (III)CONFIRMATION OF THE PRESENCE OF α-HELICAL CONFORMATION IN ANTHERAEA PERNYI SILK FIBROIN
  • 第3報 柞蚕フィブロインにおけるα-Helixの確認

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Abstract

The presence of α-helical conformation in Antheraea pernyi silk fibroin was confirmed by means of X-ray diffractometry, infrared spectroscopy and optical rotatory dispersion as follows:<br>1. Spacings of 7.4 and 3.7A in the X-ray patterns of fibroin gel are correspond to the twe specific leading spacings in the powder diagram of α-helical poly-L-alanine.<br>2. In Amide V region of IRS, the fibroin film gives 620cm-1 band typical of α-helix as well as 650cm-1 band typical of random coil, both diminishes in their intensity upon deuteration.<br>3. The fibroin in aqueous solution at neutral pH shows the Cotton effects typical of α-helix, atrough at 232mμ and a peak at 198mμ with a shoulder arround 210mμ. The he_??_cal content is 10 to 20%.

Journal

  • Sen'i Gakkaishi

    Sen'i Gakkaishi 23 (7), 311-315, 1967

    The Society of Fiber Science and Technology, Japan

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