University of Vienna, Faculty of Chemistry, Department of Computational Biological Chemistry, Währingerstr. 17, A-1090 Vienna, Austria.
Phys Chem Chem Phys. 2018 Jul 25;20(29):19581-19594. doi: 10.1039/c8cp02360c.
Recent experiments by Weingärtner et al. have given a first hint that dielectric spectroscopy is able to yield a quantitative measure of inter-protein mutual orientation. Therefore, in this computational study, we investigate crowded multi-protein solutions with a special focus on this mutual orientation and its context with dielectric spectroscopy. To the end, existing standard force fields had to be improved by re-scaling the dispersion interaction between protein and water. We find that proper hydration has a strong influence on inter-protein correlations as an enhancement of protein hydration by 10% has a great impact on orientational intermolecular structure. Altogether, the crowding behaviour is improved considerably.
最近，Weingärtner 等人的实验首次表明，介电谱能够定量测量蛋白质之间的相互取向。因此，在这项计算研究中，我们研究了拥挤的多蛋白溶液，特别关注这种相互取向及其与介电谱的关系。为此，必须通过重新调整蛋白质和水之间的色散相互作用来改进现有的标准力场。我们发现适当的水合作用对蛋白质间的相关性有很强的影响，因为增加 10%的蛋白质水合作用会对取向的分子间结构产生很大的影响。总的来说，拥挤行为得到了很大的改善。
