...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of biochemical and molecular toxicology >A study on the interaction between cadmium and alpha-chymotrypsin and the underlying mechanisms
【24h】

A study on the interaction between cadmium and alpha-chymotrypsin and the underlying mechanisms

机译：镉和α-chymotrypsin与潜在机制相互作用的研究

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

Because cadmium might interact with proteins and, thus, exert toxicity in organisms, it is vital to understand the molecular mechanism of the interaction between cadmium and biologically relevant proteins as well as the structural and functional changes in these proteins. In this study, the interaction between alpha-chymotrypsin (alpha-ChT) and cadmium chloride (CdCl2) was investigated by performing enzyme activity determinations, multispectroscopic measurements, isothermal titration calorimetry, and molecular docking studies. It was demonstrated that CdCl2 binds to alpha-ChT mainly via electrostatic forces with (21.0 +/- 0.982) binding sites, leading to the increase of alpha-helix and the decrease of beta-sheet. The interaction between CdCl2 and alpha-ChT loosened the protein skeleton and increased the molecular volume of alpha-ChT. CdCl2 first binds to the interface of alpha-ChT and then interacts with the key residues His 57 or Asp 102 or both in the active sites, leading to the activity inhibition of alpha-ChT under the exposure of high CdCl2 concentrations.
机译：因为镉可能与蛋白质相互作用，因此，在生物体中施加毒性，了解镉和生物相关蛋白质之间相互作用的分子机制至关重要，以及这些蛋白质中的结构和功能变化。在该研究中，通过进行酶活性测定，多光谱测量，等温滴定热量和分子对接研究，研究了α-chymotrypsin（α-cht）和氯化镉（CdCl2）之间的相互作用。结果证明，CDCl2主要通过静电力与（21.0 +/- 0.982）结合位点的静电力结合，导致α-螺旋的增加和β-片的减少。 CDCL2和α-CHT之间的相互作用松开了蛋白质骨架并增加了α-CHT的分子量。 CDCl2首先与α-CHT的界面结合，然后用钥匙残留物与其57或ASP 102或两者相互作用，从而在高CDCl2浓度的暴露下的α-CHT的活性抑制。

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