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Hirose S.,Japan National Institute of Advanced Industrial Science and Technology | Kawamura Y.,Japan Biological Informatics Consortium JBiC | Yokota K.,Japan National Institute of Advanced Industrial Science and Technology | Kuroita T.,Toyobo Ltd | And 7 more authors.
Journal of Biochemistry | Year: 2011

Recombinant protein technology is an important tool in many industrial and pharmacological applications. Although the success rate of obtaining soluble proteins is relatively low, knowledge of protein expression/solubility under 'standard' conditions may increase the efficiency and reduce the cost of proteomics studies. In this study, we conducted a genome-scale experiment to assess the overexpression and the solubility of human full-length cDNA in an in vivo Escherichia coli expression system and a wheat germ cell-free expression system. We evaluated the influences of sequence and structural features on protein expression/solubility in each system and estimated a minimal set of features associated with them. A comparison of the feature sets related to protein expression/solubility in the in vivo Escherichia coli expression system revealed that the structural information was strongly associated with protein expression, rather than protein solubility. Moreover, a significant difference was found in the number of features associated with protein solubility in the two expression systems. © The Authors 2011. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved. Source

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