Water-Mediated Dimerization of Ubiquitin Ions Captured by Cryogenic Ion Mobility-Mass Spectrometry,The Journal of Physical Chemistry Letters

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Water-Mediated Dimerization of Ubiquitin Ions Captured by Cryogenic Ion Mobility-Mass Spectrometry
The Journal of Physical Chemistry Letters ( IF 4.8 ) Pub Date : 2015-12-03 00:00:00 , DOI: 10.1021/acs.jpclett.5b02382
Kelly A. Servage ₁ , Joshua A. Silveira ₁ , Kyle L. Fort ₁ , David E. Clemmer ₂ , David H. Russell ₁

Affiliation

The dynamics, structures, and functions of most biological molecules are strongly influenced by the nature of the peptide’s or protein’s interaction with water. Here, cryogenic ion mobility-mass spectrometry studies of ubiquitin have directly captured a water-mediated protein–protein binding event involving hydrated, noncovalently bound dimer ions in solution, and this interaction has potential relevance to one of the most important protein–protein interactions in nature. As solvent is removed, dimer ions, viz. [2 M + 14H]¹⁴⁺, can be stabilized by only a few attached water molecules prior to dissociation into individual monomeric ions. The hydrophobic patch of ubiquitin formed by the side chains of Leu-8, Ile-44, and Val-70 meet all the necessary conditions for a protein–protein binding “hot spot,” including the requirement for occlusion of water to nearby hydrophilic sites, and it is suggested that this interaction is responsible for formation of the hydrated noncovalent ubiquitin dimer.

中文翻译：

低温离子淌度-质谱法捕获的泛素离子水介导的二聚化

大多数生物分子的动力学，结构和功能受肽或蛋白质与水相互作用的性质的强烈影响。在这里，泛素的低温离子淌度-质谱研究直接捕获了水介导的蛋白质-蛋白质结合事件，涉及溶液中水合的，非共价结合的二聚体离子，这种相互作用与最重要的蛋白质-蛋白质相互作用之一具有潜在的相关性。自然。随着溶剂的去除，二聚离子也就是。[2 M + 14H] ¹⁴⁺在离解成单个单体离子之前，仅需几个附着的水分子即可稳定。由Leu-8，Ile-44和Val-70的侧链形成的泛素疏水补丁满足蛋白质-蛋白质结合“热点”的所有必要条件，包括要求将水闭塞到附近的亲水位点，并建议这种相互作用是导致水合非共价泛素二聚体形成的原因。

更新日期：2015-12-03

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