Li S F, McGhie A J, Tang S L
DuPont Central Research and Development, Experimental Station, Wilmington, Delaware 19880-0356.
Biophys J. 1994 Apr;66(4):1209-12. doi: 10.1016/S0006-3495(94)80903-8.
Atomic force microscopy was used to study the three-dimensional nanometer-scale structure of the dragline silk of Nephila clavipes from microtomed sections of the silk. Contrary to a previously proposed model of randomly distributed protein crystallites interspersed in amorphous regions, a highly organized skin-core structure of the fiber was observed. The skin appeared to be thin with no discernible distinct features. The core consists of pleated fibril-like structures, which are arranged in two concentric cylinders. Upon stretching, the pleats were smoothed out substantially. The mechanical properties of spider silk can quite straightforwardly be related to the newly observed structures.
利用原子力显微镜从蜘蛛丝的切片中研究了大木林蜘蛛（Nephila clavipes）拖牵丝的三维纳米级结构。与之前提出的随机分布的蛋白质微晶散布在无定形区域的模型相反，观察到纤维具有高度有序的皮芯结构。皮层似乎很薄，没有明显的特征。芯层由褶皱的纤维状结构组成，这些结构排列成两个同心圆柱。拉伸时，褶皱基本变平。蜘蛛丝的机械性能可以很直接地与新观察到的结构联系起来。
