Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

Das R.K.; Pappu R.V.

首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

【24h】

Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

机译：Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

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

The functions of intrinsically disordered proteins (IDPs) are governed by relationships between information encoded in their amino acid sequences and the ensembles of conformations that they sample as autonomous units. Most IDPs are polyampholytes, with sequences that include both positively and negatively charged residues. Accordingly, we focus here on the sequence- ensemble relationships of polyampholytic IDPs. The fraction of charged residues discriminates between weak and strong polyampholytes. Using atomistic simulations, we show that weak polyampholytes form globules, whereas the conformational preferences of strong polyampholytes are determined by a combination of fraction of charged residues values and the linear sequence distributions of oppositely charged residues. We quantify the latter using a patterning parameter ? that lies between zero and one. The value of ? is low for well-mixed sequences, and in these sequences, intrachain electrostatic repulsions and attractions are counterbalanced, leading to the unmasking of preferences for conformations that resemble either self-avoiding random walks or generic Flory random coils. Segregation of oppositely charged residues within linear sequences leads to high ?-values and preferences for hairpin-like conformations caused by long-range electrostatic attractions induced by conformational fluctuations. We propose a scaling theory to explain the sequence-encoded conformational properties of strong polyampholytes.We show that naturally occurring strong polyampholytes have low ?-values, and this feature implies a selection for random coil ensembles. The design of sequences with different ?-values demonstrably alters the conformational preferences of polyampholytic IDPs, and this ability could become a useful tool for enabling direct inquiries into connections between sequence-ensemble relationships and functions of IDPs.

著录项

来源
《Proceedings of the National Academy of Sciences of the United States of America》 |2013年第33期|13392-13397|共6页
作者
Das R.K.; Pappu R.V.;
展开▼
作者单位

Department of Biomedical Engineering, Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130, United States;

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
intrinsically disordered proteins; linear sequence distributions; oppositely charged residues;

Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

摘要

著录项

相关主题

期刊订阅