Sequence-Based Prediction of Protein Solubility

被引：81

作者：

Agostini, Federico ^{[2
,3
]}

Vendruscolo, Michele ^{[1
]}

Tartaglia, Gian Gaetano ^{[2
,3
]}

机构：

[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

[2] CRG, Barcelona 08003, Spain

[3] UPF, Barcelona 08003, Spain

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2012年 / 421卷 / 2-3期

基金：

英国惠康基金;

关键词：

protein aggregation; protein solubility; protein folding; E. coli proteome; AGGREGATION PROPERTIES; EXPRESSION LEVELS; CONTACT ORDER; DETERMINANTS; STABILITY; REGIONS; RATES; PRONE;

D O I：

10.1016/j.jmb.2011.12.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：237 / 241

页数：5

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