Liaison amid disorder: non-native interactions may underpin long-range coupling in proteins.

Journal of Biology Pub Date : 2009-01-01 Epub Date: 2009-03-13 DOI:10.1186/jbiol126
Hue Sun Chan, Zhuqing Zhang
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引用次数: 6

Abstract

A lattice-model study of double-mutant cycles published in BMC Structural Biology underscores how interactions in non-native conformations can lead to thermodynamic coupling between distant residues in globular proteins, adding to recent advances in delineating the often crucial roles played by disordered conformational ensembles in protein behavior.

无序中的联系:非原生相互作用可能支持蛋白质的远程偶联。
发表在《BMC结构生物学》上的一项关于双突变周期的晶格模型研究强调了非天然构象中的相互作用如何导致球状蛋白中远端残基之间的热力学耦合,增加了最近在描述无序构象集成在蛋白质行为中所起的关键作用方面的进展。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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