• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Proteome-level interplay between folding and aggregation propensities of proteins.
【24h】

Proteome-level interplay between folding and aggregation propensities of proteins.

机译：蛋白质折叠和聚集倾向之间的蛋白质组水平相互作用。

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

With the advent of proteomics, there is an increasing need of tools for predicting the properties of large numbers of proteins by using the information provided by their amino acid sequences, even in the absence of the knowledge of their structures. One of the most important types of predictions concerns whether proteins will fold or aggregate. Here, we study the competition between these two processes by analyzing the relationship between the folding and aggregation propensity profiles for the human and Escherichia coli proteomes. These profiles are calculated, respectively, using the CamFold method, which we introduce in this work, and the Zyggregator method. Our results indicate that the kinetic behavior of proteins is, to a large extent, determined by the interplay between regions of low folding and high aggregation propensities.
机译：随着蛋白质组学的到来，越来越需要用于通过使用蛋白质氨基酸序列提供的信息来预测大量蛋白质特性的工具，即使在不了解其结构的情况下。最重要的预测类型之一是蛋白质会折叠还是聚集。在这里，我们通过分析人类和大肠杆菌蛋白质组的折叠和聚集倾向图之间的关系，研究了这两个过程之间的竞争。这些配置文件分别使用我们在本文中介绍的CamFold方法和Zyggregator方法进行计算。我们的结果表明，蛋白质的动力学行为在很大程度上取决于低折叠和高聚集倾向区域之间的相互作用。

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