• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Diversity of molecular transformations involved in the formation of spider silks.
【24h】

Diversity of molecular transformations involved in the formation of spider silks.

机译：蜘蛛丝形成过程中涉及的分子转化的多样性。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Spiders that spin orb webs secrete seven types of silk. Although the spinning process of the dragline thread is beginning to be understood, the molecular events that occur in spiders' opisthosomal glands, which produce the other fibers, are unknown due to a lack of data regarding their initial and final structures. Taking advantage of the efficiency of Raman spectromicroscopy in investigating micrometer-sized biological samples, we have determined the secondary structure of proteins in the complete set of glands of the orb-weaving spider Nephila clavipes. The major and minor ampullate silks in the sac of their glands have identical secondary structures typical of natively unfolded proteins. Spidroins are converted into fibers containing highly oriented beta-sheets. The capture spiral represents a distinct structural singleton. The proteins are highly disordered prior to spinning and undergo no molecular change or alignment upon spinning. The cylindrical, aciniform, and piriform proteins are folded in their initial state with a predominance of alpha-helices, but whereas the cylindrical gland forms a fiber similar to the major ampullate thread, the aciniform and piriform glands produce fibers dominated by moderately oriented beta-sheets and alpha-helices. The conformation of the proteins before spinning is related to intrinsic characteristics of their primary structure. Proteins that are unfolded in the gland have repeat sequences composed of submotifs and display no sequence regions with aggregation propensity. By contrast, the folded proteins have neither submotifs nor aggregation-prone sequence regions. Taken together, the Raman data show a remarkable diversity of molecular transformations occurring upon spinning.
机译：旋转球网的蜘蛛会分泌七种丝绸。尽管人们开始了解拉铲丝的纺丝过程，但是由于缺乏有关其初始和最终结构的数据，在产生其他纤维的蜘蛛的阿胶体腺中发生的分子事件是未知的。利用拉曼光谱学在研究微米级生物样品中的效率，我们确定了球形编织蜘蛛Nephila锁骨的完整腺体中蛋白质的二级结构。腺囊中的主要壶腹丝和次要壶腹丝具有相同的二级结构，这些二级结构通常是天然未折叠的蛋白质。螺旋蛋白被转化为含有高度取向的β-折叠的纤维。捕获螺旋表示一个独特的结构单例。蛋白质在旋转前高度无序，在旋转时不会发生分子变化或对齐。圆柱状，腺状和梨状蛋白质在初始状态下会折叠，并具有主要的α螺旋结构，但是圆柱状腺体形成的纤维类似于壶腹螺纹，而腺状和梨状腺产生的纤维则以中等方向的β-螺旋为主床单和alpha螺旋。纺丝前蛋白质的构象与其一级结构的固有特征有关。在腺体中展开的蛋白质具有由亚基组成的重复序列，并且没有显示具有聚集倾向的序列区域。相比之下，折叠的蛋白质既没有亚基也没有易于聚集的序列区域。综上所述，拉曼数据显示出纺丝时发生的分子转化的显着多样性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号