首页> 外文会议>Pacific symposium on biocomputing >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:组合多序列减少蛋白质模型方法预测小蛋白的三级结构

获取原文

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成从头折叠模拟中,测试组20种nonhomiologous蛋白质的低resolutionteriary结构已经predited。这些蛋白,其代表所有二级结构类型,包含从37到100个残基。二级结构的限制是由结合了多种序列信息的PHD次级struture预测算法提供的。预测叔限制从多个序列比对通过两步骤方法获得:首先,“种子”侧链触头由相关突变的分析,鉴定,然后,种子触点通过逆折叠algorith“膨胀”。然后,这些预测约束掺入晶格系,降低的蛋白质模型。取决于折叠的复杂性,resuulting nativelike拓扑表现出坐标根均方推导,cRMSD,从3.1和6.7 A.总体之间天然的,这项研究表明,使用约束的从多重序列比对与折叠组件算法相结合衍生是preomising方法小蛋白质的全局拓扑的预测。

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