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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Adhesive-cohesive model for protein compressibility: An alternative perspective on stability
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Adhesive-cohesive model for protein compressibility: An alternative perspective on stability

机译：蛋白质可压缩性的胶粘-内聚模型：稳定性的另一种观点

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摘要

As a dynamic property of folded proteins, protein compressibility provides important information about the forces that govern structural stability. We relate intrinsic compressibility to stability by using molecular dynamics to identify a molecular basis for the variation in compressibility among globular proteins. We find that excess surface charge accounts for this variation not only for the proteins simulated by molecular dynamics but also for a larger set of globular proteins. This dependence on charge distribution forms the basis for an adhesive-cohesive model of protein compressibility in which attractive forces from solvent compete with tertiary interactions that favor folding. Further, a newly recognized correlation between compressibility and the heat capacity of unfolding infers a link between compressibility and the enthalpy of unfolding. This linkage, together with the adhesive-cohesive model for compressibility, leads to the conclusion that folded proteins can gain enthalpic stability from a uniform distribution of charged atoms, as opposed to partitioning charge to the protein surface. Whether buried charged groups can be energetically stabilizing is a fundamental, yet controversial, question regarding protein structure. The analysis reported here implies that one mechanism to gain enthalpic stability involves positioning charge inside the protein in an optimal structural arrangement.
机译：作为折叠蛋白的动态特性，蛋白可压缩性提供了有关控制结构稳定性的力的重要信息。我们通过使用分子动力学来识别球状蛋白之间可压缩性变化的分子基础，从而将固有可压缩性与稳定性联系起来。我们发现，过量的表面电荷不仅是通过分子动力学模拟的蛋白质而且是较大的一组球状蛋白质的原因。这种对电荷分布的依赖性形成了蛋白质可压缩性的胶粘性模型的基础，其中来自溶剂的吸引力与有利于折叠的第三级相互作用竞争。此外，新近认识到的可压缩性与展开热容量之间的相关性推断出可压缩性与展开焓之间的联系。这种联系，再加上用于可压缩性的粘合剂-内聚模型，得出的结论是，折叠的蛋白质可以从带电原子的均匀分布中获得焓稳定性，而不是将电荷分配到蛋白质表面。关于埋藏的带电基团是否可以在能量上稳定是一个关于蛋白质结构的基本但有争议的问题。此处报道的分析表明，获得焓稳定性的一种机制涉及以最佳结构排列方式将蛋白质内部的电荷定位。

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