Universality of protein reentrant condensation in solution induced by multivalent metal ions

Universality of protein reentrant condensation in solution induced by multivalent metal ions
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多价金属离子诱导溶液中蛋白质重入缩合的普遍性

DOI:
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发表时间:
2010
期刊:
Proteins: Structure, Function, and Bioinformatics
影响因子:
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通讯作者:
F. Schreiber
F. Schreiber
中科院分区:
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文献类型:
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作者:
Fajun Zhang;S. Weggler;M. Ziller;L. Ianeselli;B. Heck;A. Hildebrandt;O. Kohlbacher;M. Skoda;R. Jacobs;F. Schreiber

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由于蛋白质表面复杂的电荷模式和不规则的几何形状,蛋白质溶液在强静电耦合条件下的有效相互作用和相行为很难理解。这使它们有别于DNA或传统胶体等相关系统。在这项工作中,我们讨论了蛋白质在溶液中由多价反离子引起的折入缩合(RC)的普遍性问题,即最近发现的在相分离后添加更多盐时的再溶解问题(Zhang等,Phys Rev Lett 2008;101:148101)。这一讨论是基于对具有不同电荷模式的五种不同蛋白质和五种不同的多价反离子的系统研究。Zeta电位测量证实了蛋白质在重入区通过与多价反离子结合而有效的电荷反转,这一点得到了蒙特卡罗模拟的支持。三价阳离子的电荷反转需要蛋白质的整体负净电荷。对一组有代表性的蛋白质序列的统计分析表明,从理论上讲,大约一半的蛋白质都有可能产生这种效应。我们的结果可用于控制蛋白质的相行为,特别是促进蛋白质结晶。蛋白质2010年。©2010 Wiley-Liss公司。
The effective interactions and phase behavior of protein solutions under strong electrostatic coupling conditions are difficult to understand due to the complex charge pattern and irregular geometry of protein surfaces. This distinguishes them from related systems such as DNA or conventional colloids. In this work, we discuss the question of universality of the reentrant condensation (RC) of proteins in solution induced by multivalent counterions, i.e., redissolution on adding further salts after phase separation, as recently discovered (Zhang et al., Phys Rev Lett 2008; 101:148101). The discussion is based on a systematic investigation of five different proteins with different charge patterns and five different multivalent counterions. Zeta potential measurements confirm the effective charge inversion of proteins in the reentrant regime via binding of multivalent counterions, which is supported by Monte Carlo simulations. Charge inversion by trivalent cations requires an overall negative net charge of the protein. Statistical analysis of a representative set of protein sequences reveals that, in theory, this effect could be possible for about half of all proteins. Our results can be exploited for the control of the phase behavior of proteins, in particular facilitating protein crystallization. Proteins 2010. © 2010 Wiley‐Liss, Inc.
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