書誌事項
- タイトル別名
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- Comprehensive Analysis of Aggregation Propensity and Chaperone Effects for All <i>Escherichia coli</i> Proteins
- 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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抄録
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>
収録刊行物
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- 生物物理
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生物物理 53 (6), 309-312, 2013
一般社団法人 日本生物物理学会
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詳細情報 詳細情報について
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- CRID
- 1390282681511281792
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- NII論文ID
- 10031203607
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- NII書誌ID
- AN00129693
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- COI
- 1:CAS:528:DC%2BC3sXhvVGqsb3L
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- ISSN
- 13474219
- 05824052
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- NDL書誌ID
- 025052491
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可