The research work of this project was focused on the comprehensive mechanical properties of animal silk (i.e. spider major ampullate silk and Bombyx mori silkworm silk etc), and the self-assembling behaviors as well as the conformation of silk proteins and its transition in varied conditions. Based on the fruitful results, we conclude that on a more advanced level, the condensed state of a silk fiber (i.e. the orientation of its molecular chains) as well as its secondary structure (such as fibrillar structures and skin-core morphology) is also determined by the interaction of the spinning process with the state of the proteins in the silk gland, besides the amino acid sequences of silk proteins. Thus the unique mechanical behaviors of spider (as silkworm) silk is controlled not only by the silk protein genes, but as much (if not more) also by the processes and the environment in which these are assembled into the silk filament. It is hoped this point of view will appeal to biologists working on the spider and silkworm silk, to material scientists and to biotechnologists who are attamping to genetically engeer proteins for the production of manmade silk-like protein.
在进一步了解主腺蜘蛛丝综合特性的基础上,研究蜘蛛丝及其体内丝蛋白的超分子结构与它潜硐中阅苤涞墓叵?通过对蜘蛛吐丝机理的充分认识,结合再生蛋白纤维的制备和性能比?阐明此类蛋白质分子在溶液中自组装过程的本质及驱动力控制因素,以次解释蜘蛛丝蛋白亩?三级结构在一定条件下的可变型(可控性)和在决定蜘蛛丝最终特性中的重要性.
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数据更新时间:2023-05-31
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