• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Fast Compaction of alpha-Lactalbumin During Folding Studied by Stopped-flow X-ray Scattering.
【24h】

Fast Compaction of alpha-Lactalbumin During Folding Studied by Stopped-flow X-ray Scattering.

机译：通过停止流X射线散射研究折叠过程中α-乳清蛋白的快速压实。

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

To monitor the fast compaction process during protein folding, we have used a stopped-flow small-angle X-ray scattering technique combined with a two-dimensional charge-coupled device-based X-ray detector that makes it possible to improve the signal-to-noise ratio of data dramatically, and measured the kinetic refolding reaction of alpha-lactalbumin. The results clearly show that the radius of gyration and the overall shape of the kinetic folding intermediate of alpha-lactalbumin are the same as those of the molten globule state observed at equilibrium. Thus, the identity between the kinetic folding intermediate and the equilibrium molten globule state is firmly established. The present results also suggest that the folding intermediate is more hydrated than the native state and that the hydrated water molecules are dehydrated when specific side-chain packing is formed during the change from the molten globule to the native state.
机译：为了监控蛋白质折叠过程中的快速压紧过程，我们使用了一种停止流动的小角度X射线散射技术，并结合了基于二维电荷耦合器件的X射线检测器，从而可以改善信号数据的高信噪比，并测量了α-乳白蛋白的动力学重折叠反应。结果清楚地表明，α-乳白蛋白的旋转半径和动力学折叠中间体的整体形状与在平衡时观察到的熔融球状状态相同。因此，牢固地建立了动力学折叠中间体与平衡熔融小球状态之间的同一性。本结果还表明，折叠中间体比天然状态更易水合，并且当从熔融小球转变为天然状态时形成特定的侧链堆积时，水合的水分子会脱水。

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