首页> 外文会议>Pacific Symposium on Biocomputing '98 4-9 January 1998 Maui, Hawaii, USA >Combined multiple sequence reduced protein model approach to predict the tertiary structure of small proteins
【24h】

Combined multiple sequence reduced protein model approach to predict the tertiary structure of small proteins

机译:结合多序列还原蛋白模型方法预测小蛋白的三级结构

获取原文
获取原文并翻译 | 示例

摘要

By incorporating predicted secondary and tertiary restraints into ab initio folding simulations, low resolutionteriary structures of a test set of 20 nonhomiologous proteins have been predited. These proteins, which represent all secondary structural classes, contain from 37 to 100 residues. Secondary structural restraints are provided by the PHD secondary struture prediction algorithm that incorporates multiple sequence information. Predicted tertiary restraints are obtained from multiple sequence alignments via a two-step process: First, "seed" side chain contacts are identified from a correlated mutation analysis, and then, the seed contacts are "expanded" by an inverse folding algorith. These predicted restraints are then incorporated into a lattice based, reduced protein model. Depending upon fold complexity, the resuulting nativelike topologies exhibit a coordinate root-mean-square derivation, cRMSD, from native between 3.1 and 6.7 A. Overall, this study suggests that the use of restraints derived from multiple sequence alignments combined with a fold assembly algorithm is a preomising approach to the prediction of the global topology of small proteins.
机译:通过将预测的二级和三级约束纳入从头算起的折叠模拟中,已经确定了20种非同源蛋白质测试集的低分辨率结构。这些蛋白质代表所有二级结构类别,包含37至100个残基。 PHD二级结构预测算法提供了二级结构约束,该算法结合了多个序列信息。可以通过两步过程从多个序列比对中获得预测的第三类限制条件:首先,从相关的突变分析中识别“种子”侧链接触,然后通过反向折叠算法“扩展”种子接触。然后将这些预测的约束条件并入基于格的还原蛋白质模型中。根据折叠的复杂程度,重新生成的类似自然的拓扑在3.1和6.7 A之间表现出从原始坐标的均方根坐标cRMSD。总的来说,这项研究表明,使用源自多重序列比对的约束结合折叠组装算法是预测小蛋白全局拓扑结构的一种先决方法。

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