• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>RSC Advances >Relaxation dynamics in lens crystallin proteins: a dielectric and thermodynamic approach using TDR
【24h】

Relaxation dynamics in lens crystallin proteins: a dielectric and thermodynamic approach using TDR

机译：晶状体晶体蛋白中的弛豫动力学：使用TDR的介电和热力学方法

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

Dielectric relaxation of water in biological systems, such as proteins and DNA, can often be described by two different time constants, one in the picosecond and the other in the nanosecond regime. In the present work, we report the temperature dependence of the relaxation dynamics, dielectric permittivity (epsilon') and loss (epsilon '') of aqueous lens proteins (crystalline) in the goat eye lens. The measurements have been carried out in the frequency range from 10 MHz to 20 GHz using TDR and in the temperature region from 298.15 K to 278.15 K. We analyse the three dispersion regions commonly found in protein solutions, usually termed beta-, gamma- and delta-relaxation. The beta-relaxation, occurring in the frequency range between 70 and 100 MHz, and the gamma-relaxation between 15 and 18 GHz can be attributed to the rotation of the polar protein molecules in their aqueous medium and the reorientational motion of the free water molecules respectively. The nature of delta-relaxation, which is often ascribed to the motion of bound water molecules, is not yet fully understood. Here, we provide data on the temperature dependence of dielectric and thermodynamic parameters of all three detected processes, beta-, gamma- and delta-relaxation. We found significant temperature dependence of the dielectric and thermodynamic parameters of the aqueous proteins, indicating conformational changes.
机译：诸如蛋白质和DNA之类的生物系统中水的介电弛豫通常可以通过两个不同的时间常数来描述，一个在皮秒内，另一个在纳秒内。在本工作中，我们报告了山羊眼晶状体中水晶状体蛋白（晶体）的弛豫动力学，介电常数（ε）和损耗（ε”）的温度依赖性。使用TDR在10 MHz至20 GHz的频率范围内以及298.15 K至278.15 K的温度范围内进行了测量。我们分析了蛋白质溶液中常见的三个分散区，通常称为β-，γ-和三角松弛。发生在70至100 MHz频率范围内的β松弛，以及发生在15至18 GHz之间的γ松弛，可归因于极性蛋白质分子在其水性介质中的旋转以及自由水分子的重新定向运动分别。 δ松弛的性质通常归因于结合的水分子的运动，但尚未完全了解。在这里，我们提供有关所有三个检测到的过程（β，γ和δ弛豫）的介电常数和热力学参数与温度的相关性的数据。我们发现水性蛋白质的介电和热力学参数对温度的显着依赖性，表明其构象变化。

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