書誌事項
- タイトル別名
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- STUDIES ON THE FINE STRUCTURE OF SILKFIBROIN
- 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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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%.
収録刊行物
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- 繊維学会誌
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繊維学会誌 23 (7), 311-315, 1967
社団法人 繊維学会
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詳細情報 詳細情報について
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- CRID
- 1390001204864371712
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- NII論文ID
- 130004202134
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- NII書誌ID
- AN00131651
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- COI
- 1:CAS:528:DyaF2sXltV2jsr0%3D
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- ISSN
- 18842259
- 00379875
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- NDL書誌ID
- 8279242
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- データソース種別
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- JaLC
- NDL
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- 抄録ライセンスフラグ
- 使用不可