...
首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Dynamics of compact denatured states of glutaminyl-tRNA synthetase probed by bis-ANS binding kinetics
【24h】

Dynamics of compact denatured states of glutaminyl-tRNA synthetase probed by bis-ANS binding kinetics

机译:bis-ANS结合动力学探测的谷氨酰胺-tRNA合成酶的致密变性状态的动力学。

获取原文
获取原文并翻译 | 示例
           

摘要

Bis-ANS binds to native glutaminyl-tRNA synthetase (GlnRS) with a fast and a slow phase. The rate constant of the slow phase is independent of bis-ANS concentration suggesting a slow conformational change in the pathway of bis-ANS binding. Aging of GlnRS causes a large decrease of the slow phase amplitude with concomitant increase of the fast phase amplitude. Several other large, multi-domain proteins show similar patterns upon aging. The near UV-CD spectra of the native and the aged GlnRS remain similar. Significant changes in far UV-CD, acrylamide quenching and sulfhydryl reactivity, are seen upon aging, suggesting disruptions in native interactions. Refolding of GlnRS from the urea-denatured state rapidly produces a state that is very similar to the equilibrium molten globule state. Bis-ANS binds to the molten globule state with kinetics similar to that of the aged state and unlike that of the native state. This suggests that the slow binding phase of bis-ANS, seen in native proteins, originate from relatively high energy barriers between the native and the more open states. Thus bis-ANS can be used as a powerful probe for large amplitude, low-frequency motions of proteins. (C) 2000 Elsevier Science B.V. All rights reserved. [References: 26]
机译:Bis-ANS以快慢相结合至天然谷氨酰胺-tRNA合成酶(GlnRS)。慢相的速率常数与bis-ANS浓度无关,表明bis-ANS结合途径的构象缓慢变化。 GlnRS的老化会导致慢速相位幅度大大降低,而快速相位幅度则随之增加。其他几种大型的多结构域蛋白质在衰老时也显示出相似的模式。天然的和衰老的GlnRS的近UV-CD光谱保持相似。老化后,可以看到远紫外线-CD,丙烯酰胺猝灭和巯基反应性发生了显着变化,表明天然相互作用被破坏。 GlnRS从尿素变性状态快速重折叠会产生一种非常类似于平衡熔融小球状态的状态。 Bis-ANS以类似于衰老状态的动力学且不同于天然状态的动力学结合到熔融的球状状态。这表明在天然蛋白质中看到的bis-ANS的缓慢结合阶段源自天然状态和开放状态之间相对较高的能垒。因此,bis-ANS可以用作蛋白质大幅度,低频运动的有力探针。 (C)2000 Elsevier Science B.V.保留所有权利。 [参考:26]

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