Comprehensive Analysis of Aggregation Propensity and Chaperone Effects for All <i>Escherichia coli</i> Proteins

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  • NIWA Tatsuya
    Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
  • UEDA Takuya
    Graduate School of Frontier Sciences, University of Tokyo
  • TAGUCHI Hideki
    Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology

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  • 大腸菌全タンパク質の凝集性とシャペロン効果の網羅的な解析
  • ダイチョウキン ゼン タンパクシツ ノ ギョウシュウセイ ト シャペロン コウカ ノ モウラテキ ナ カイセキ

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Abstract

Protein folding is often hampered by protein aggregation, which can be prevented by a variety of chaperones in the cell. However, the relationship between the propensity to form aggregates and primary sequence and preferences of chaperones for substrates has not been understood. We comprehensively analyzed the aggregation propensity of all Escherichia coli proteins and the aggregation prevention effect of three major chaperones for aggregation-prone proteins by using a reconstituted chaperone-free translation system (PURE system). The resource obtained here can be used to investigate the properties of proteins of interest in terms of their solubilities and chaperone effects.<br>

Journal

  • Seibutsu Butsuri

    Seibutsu Butsuri 53 (6), 309-312, 2013

    The Biophysical Society of Japan General Incorporated Association

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