...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Is Protein Folding Rate Dependent on Number of Folding Stages? Modeling of Protein Folding with Ferredoxin-Like Fold
【24h】

Is Protein Folding Rate Dependent on Number of Folding Stages? Modeling of Protein Folding with Ferredoxin-Like Fold

机译：蛋白质折叠率取决于折叠阶段数吗？铁氧还蛋白样折叠的蛋白质折叠建模

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

Statistical analysis of protein folding rates has been done for 84 proteins with available experimental data. A surprising result is that the proteins with multi-state kinetics from the size range of 50-100 amino acid residues (a.a.) fold as fast as proteins with two-state kinetics from the same size range. At the same time, the proteins with two-state kinetics from the size range 101-151 a.a. fold faster than those from the size range 50-100 a.a. Moreover, it turns out unexpectedly that usually in the group of structural homologs from the size range 50-100 a.a., proteins with multi-state kinetics fold faster than those with two-state kinetics. The protein folding for six proteins with a ferredoxin-like fold and with a similar size has been modeled using Monte Carlo simulations and dynamic programming. Good correlation between experimental folding rates, some structural parameters, and the number of Monte Carlo steps has been obtained. It is shown that a protein with multi-state kinetics actually folds three times faster than its structural homologs.
机译：已经对84种蛋白质的蛋白质折叠率进行了统计分析，并提供了可用的实验数据。令人惊讶的结果是，具有50-100个氨基酸残基（a.a.）大小范围的多态动力学的蛋白质的折叠速度与具有相同大小范围的两种态动力学的蛋白质的折叠速度一样快。同时，蛋白质具有101-151 a.a范围内的二态动力学。折叠速度比尺寸范围为50-100 a.a.而且，出乎意料地发现，通常在大小范围为50-100a.a。的结构同系物组中，具有多态动力学的蛋白质比具有二态动力学的蛋白质折叠更快。已经使用蒙特卡罗模拟和动态编程对六种具有铁氧还蛋白样折叠和相似大小的蛋白质进行了蛋白质折叠。实验折叠率，一些结构参数和蒙特卡洛步数之间具有良好的相关性。结果表明，具有多态动力学的蛋白质的折叠速度实际上是其结构同源物的三倍。

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