A Cuboid Spider Silk: Structure–Function Relationship and Polypeptide Signature
作者: Na KongFengju WanWentao DaiPing WuChen SuChao PengKe ZhengXuexin ChenShengjie LingJinkang GongYuan Yao
作者单位: 1School of Physical Science and Technology ShanghaiTech University 393 Middle Huaxia Road Pudong Shanghai 201210 China
2 Shanghai Center for Bioinformation Technology & Shanghai Engineering Research Center of Pharmaceutical Translation Shanghai Industrial Technology Institute 1278 Keyuan Road Shanghai 201203 China
3 National Facility for Protein Science in Shanghai Zhangjiang Lab Shanghai 201210 China
4 Shanghai Science Research Center Chinese Academy of Sciences Shanghai 201204 China
5 Institute of Insect Science College of Agriculture and Biotechnology Zhejiang University 310058 Hangzhou China
刊名: Macromolecular Rapid Communications, 2020, Vol.41 (6), pp.n/a-n/a
来源数据库: Wiley Journal
DOI: 10.1002/marc.201900583
关键词: ConformationCuboidEgg sac spider silkMechanical propertiesPolypeptides
原始语种摘要: Abstract(#br)A unique cuboid spider silk from the outer egg sac of Nephila pilipes , with an unusual square cross‐section, is disclosed. The structure–function relationships within this silk are first studied through structural characterization, mechanical measurement, protein conformation, and polypeptide signature of silk proteins. This silk maintains the higher stiffness property of egg sac silks, and also shows a species difference. Environmental response of the mechanical properties within this silk are observed. Synchrotron FTIR microspectroscopy is used to monitor the silk protein conformation in a single natural silk. The β‐sheet structure aligns parallel to the fiber axis with a content of 22% ± 2.6%. The de novo resulting polypeptide from the solid silk fibers are novel, and an...
全文获取路径: Wiley  (合作)

  • observed 观察到的
  • proteins 蛋白质
  • spider 电枢辐臂
  • abundant 丰富的
  • alanine 丙氨酸
  • resulting 引起的
  • alternating 交替
  • conformation 构象
  • within 在以内
  • mechanical 机械的