Toward an atomistic description of the urea-denatured state of proteins

Candotti M.; Esteban-Martín S.; Salvatella X.Orozco M.

首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Toward an atomistic description of the urea-denatured state of proteins

【24h】

Toward an atomistic description of the urea-denatured state of proteins

机译：Toward an atomistic description of the urea-denatured state of proteins

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相关主题

摘要

We present here the characterization of the structural, dynamics,and energetics of properties of the urea-denatured state of ubiquitin, a small prototypical soluble protein. By combining state-of-the-art molecular dynamics simulations with NMR and small-angle X-ray scattering data, we were able to: (i) define the unfolded state ensemble, (ii) understand the energetics stabilizing unfolded structures in urea, (iii) describe the dedifferential nature of the interactions of the fully unfolded proteins with urea and water, and (iv) characterize the early stages of protein refolding when chemically denatured proteins are transferred to native conditions. The results presented herein are unique in providing a complete picture of the chemically unfolded state of proteins and contribute to deciphering the mechanisms that stabilize the native state of proteins, as well as those that maintain them unfolded in the presence of urea.

著录项

来源
《Proceedings of the National Academy of Sciences of the United States of America》 |2013年第15期|5933-5938|共6页
作者
Candotti M.; Esteban-Martín S.; Salvatella X.Orozco M.;
展开▼
作者单位

Molecular Modelling and Bioinformatics Unit, Institute for Research in Biomedicine Barcelona, 08028 Barcelona, Spain;

展开▼
收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
Denaturing mechanism; Ensemble simulation; Protein unfolding; Random coil;

Toward an atomistic description of the urea-denatured state of proteins

摘要

著录项

相关主题

期刊订阅