首页> 外文会议>Biomedical and Health Informatics (BHI), 2012 IEEE-EMBS International Conference on >Symmetry Recurrence in protein sequence and structure with Pearson's correlation coefficients
【24h】

Symmetry Recurrence in protein sequence and structure with Pearson's correlation coefficients

机译:具有Pearson相关系数的蛋白质序列和结构的对称递归

获取原文
获取原文并翻译 | 示例

摘要

Evidence suggests that the present complex proteins may evolved from short peptide ancestors through a series of gene duplication and fusion events. In this paper, we use a modified recurrence plot method combined with Pearson correlation and dRMSD analysis to study the internal repeats in sequence and structure of left handed beta helix (LβH) fold and beta prism fold. Through our study, we find that most of the proteins in LβH fold reveal twofold repeats in both the sequence and structure, whereas only sequences of the proteins from beta prim fold show threefold repeats and the threefold repeats signal in structure is not weak. This may give some insights for the protein evolution.
机译:有证据表明,本发明的复杂蛋白可能是通过一系列基因复制和融合事件从短肽祖先进化而来的。在本文中,我们使用改进的递归绘图方法结合Pearson相关性和dRMSD分析来研究左旋β螺旋(LβH)折叠和β棱柱折叠的序列和结构的内部重复。通过我们的研究,我们发现LβH折叠中的大多数蛋白质在序列和结构上都显示出两个重复,而只有βprim折叠中的蛋白质序列显示出了三个重复,并且结构中的三个重复信号并不弱。这可能会为蛋白质进化提供一些见识。

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