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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

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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