THE STRUCTURE OF TUSSAH SILK FIBROIN (WITH A NOTE ON THE STRUCTURE OF BETA-POLY-L-ALANINE)
THE STRUCTURE OF TUSSAH SILK FIBROIN (WITH A NOTE ON THE STRUCTURE OF BETA-POLY-L-ALANINE)
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DOI：
10.1107/s0365110x5500217x
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发表时间：
1955-01-01
期刊：
影响因子：
--
通讯作者：
PAULING, L
中科院分区：
文献类型：
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作者：
MARSH, RE;COREY, RB;PAULING, L
最近，这些实验室制定了商业丝纤蛋白（Mex mot/）的详细结构（Marsh，Corey和Pauling，1955）。桑蚕丝素蛋白结构的一个显著特征是甘氨酸作为交替残基沿多肽链沿着。丝纤蛋白的另一种形式是来源于柞蚕丝（通常称为野生丝）的丝纤蛋白。以前的研究人员（Kratky & Kuriyama，1931; Trogus & Hess，1933）已经表明，尽管柞蚕丝素蛋白的X射线衍射图与从家蚕获得的图具有许多共同特征，但在几个方面有显著不同。它的化学成分也与家蚕有很大的不同（表1）。最显著的差异是甘氨酸和丙氨酸的相对量。特别地，柞蚕丝中甘氨酸的量（26.6残留%）为
A detailed structure for commercial silk fibroin (Bombyx mot/) has recently been formulated in these Laboratories (Marsh, Corey & Pauling, 1955). A prominent feature of the structure of Bombyx mori silk fibroin is the occurrence of glyeine as alternate residues along the polypeptide chains. Another form of silk fibroin is that derived from Tussah silk (commonly called wild silk). Previous investigators (Kratky & Kuriyama, 1931; Trogus & Hess, 1933) have shown that the X-ray diffraction pattern of Tussah silk fibroin, although having many features in common with the pattern obtained from Bombyx mori, is significantly different in several respects. Its chemical composition also differs from that of Bombyx mori in a very significant way (Table 1). The most striking differences are in the relative amounts of glycine and alanine. In particular, the amount of glycine in Tussah silk (26.6 residue%) is