STUDIES ON THE FINE STRUCTURE OF SILKFIBROIN

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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: 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. 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. 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%.

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