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Updated: Jul 2, 2026

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
08:32

Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo

Published on: October 23, 2016

チャペロニンの機能における閉じ込められた水の役割

Jeremy L England1, Del Lucent, Vijay S Pande

  • 1James H. Clark Center, S297, Stanford University, Stanford, California 94305, USA.

Journal of the American Chemical Society
|August 20, 2008
PubMed
まとめ

GroELのようなバクテリアのチャペロニンは,タンパク質の折り畳みに役立ちます. 折りたたみ支援は,内部表面が水を引き付ける能力と関連しており,タンパク質折りたたみ中の水密度の行動に関する新しい洞察を提供している.

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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Molecular Chaperones and Protein Folding03:00

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Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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