期刊
MOLECULAR BIOLOGY AND EVOLUTION
卷 28, 期 1, 页码 59-62出版社
OXFORD UNIV PRESS
DOI: 10.1093/molbev/msq291
关键词
protein structure evolution; structural disorder; gene duplication; neostructuralization; adaptive evolution; conformational ensemble
资金
- National Center for Research Resources [P20RR016474]
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR016474] Funding Source: NIH RePORTER
Protein structure is generally more conserved than sequence, but for regions that can adopt different structures in different environments, does this hold true? Understanding how structurally disordered regions evolve altered secondary structure element propensities as well as conformational flexibility among paralogs are fundamental questions for our understanding of protein structural evolution. We have investigated the evolutionary dynamics of structural disorder in protein families containing both orthologs and paralogs using phylogenetic tree reconstruction, protein structure disorder prediction, and secondary structure prediction in order to shed light upon these questions. Our results indicate that the extent and location of structurally disordered regions are not universally conserved. As structurally disordered regions often have high conformational flexibility, this is likely to have an effect on how protein structure evolves as spatially altered conformational flexibility can also change the secondary structure propensities for homologous regions in a protein family.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据