Sequence-Based Prediction of Protein Solubility
Sequence-Based Prediction of Protein Solubility
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DOI：
10.1016/j.jmb.2011.12.005
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发表时间：
2012-08-10
影响因子：
5.6
通讯作者：
Tartaglia, Gian Gaetano
中科院分区：
文献类型：
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作者：
Agostini, Federico;Vendruscolo, Michele;Tartaglia, Gian Gaetano
为了研究蛋白质聚集的热力学和动力学之间的关系，我们比较了蛋白质的溶解度和它们的聚集速率。通过考虑使用包含约70%的大肠杆菌蛋白质的体外重组翻译系统测量的蛋白质溶解度值的数据库，我们发现这两个量之间存在显著的相关性。这种相关性的存在表明，蛋白质天然状态相对于聚集态的热力学稳定性与分隔它们的动力学势垒密切相关。为了创造在蛋白质组水平上进行计算研究以进一步研究这一概念的可能性，我们开发了一种基于蛋白质的物理化学性质来预测蛋白质的溶解度的方法。皇冠版权所有(C)2011由爱思唯尔有限公司出版。保留所有权利。
In order to investigate the relationship between the thermodynamics and kinetics of protein aggregation, we compared the solubility of proteins with their aggregation rates. We found a significant correlation between these two quantities by considering a database of protein solubility values measured using an in vitro reconstituted translation system containing about 70% of Escherichia coli proteins. The existence of such correlation suggests that the thermodynamic stability of the native states of proteins relative to the aggregate states is closely linked with the kinetic barriers that separate them. In order to create the possibility of conducting computational studies at the proteome level to investigate further this concept, we developed a method of predicting the solubility of proteins based on their physicochemical properties. Crown Copyright (C) 2011 Published by Elsevier Ltd. All rights reserved.