...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Effects of Non-native Interactions on Frustrated Proteins Folding under Confinement
【24h】

Effects of Non-native Interactions on Frustrated Proteins Folding under Confinement

机译：非本地相互作用对监禁下令人沮丧的蛋白质折叠的影响

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

In vitro, kinetically significant non-native interactions have been identified experimentally during the folding of proteins Im7, Im9, and A39V/N53P/VSSL Fyn SH3 domain. To understand the role of non-native interactions on the folding of some frustrated proteins in chaperone, we employed native-centric models with and without additional transferable, sequence-dependent non-native hydrophobic interactions to comparatively study the folding behaviors of the three proteins confined in spherical cages. Under purely repulsive confinement, as a decrease of cavity size, the non-native interactions increase, especially in the unfolded state, enhancing the roughness of the folding energy landscape. As a result, the increase in native stability for the three proteins by the model incorporated non-native interactions (db + MJh phi model) is much smaller than that by the purely native-centric model (desolvation-barrier (db) model); the acceleration of folding simulated by the db + MJh phi model is much slower than that via the db model; in particular, the folding rate of Im7 decreases when reducing the cavity size under zero-denaturant condition. The repulsive confinement can also promote formation of specific non-native contacts in the transition state and favor more folding pathways passing through the misfolded state, leading to a higher population of the misfolded intermediate. In an attractive cage, the attractive interactions could inhibit the formation of intrachain non-native contacts and provide alternate folding pathways to the native state so that the population of the misfolded intermediate decreases when increasing the strength of attractive interaction between the substrate protein and cavity wall. This study should be helpful in general to understand how the chaperonins reshape the folding energy landscape of some frustrated proteins.
机译：在体外，在蛋白质IM7，IM9和A39V / N53P / VSSL FYN SH3结构域的折叠期间已经通过实验鉴定了动力学显着的非天然相互作用。要了解非本地相互作用对伴侣伴侣折叠的非本地相互作用的作用，我们用本土以与额外的可转移的序列依赖性非原生疏水相互作用相对研究三种蛋白质限制的折叠行为在球架上。在纯粹的排斥限制下，作为腔尺寸的减小，非天然相互作用增加，特别是在展开状态下，增强了折叠能量景观的粗糙度。结果，模型的三种蛋白质的天然稳定性的增加掺入非天然相互作用（DB + MJH PHI模型）远小于纯净以本地型号（DESolvation-Barrier（DB）模型）; DB + MJH PHI模型模拟的折叠加速度比通过DB模型的折叠速度慢得多;特别地，当在零变性状态下减小腔体尺寸时，IM7的折叠速率降低。令人厌恶的限制还可以促进过渡状态中的特定非天然接触的形成，并赞有更多的折叠途径，通过错误的状态，导致较高的被错误的中间体。在有吸引力的笼中，有吸引力的相互作用可以抑制内夹内非天然触点的形成，并为天然状态提供交替的折叠途径，使得在增加底物蛋白和腔壁之间具有吸引性相互作用的强度时，错误的中间体的群体降低。这项研究通常应该有助于了解伴侣素蛋白的重塑一些沮丧的蛋白质的折叠能量景观。

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