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Updated: Jul 27, 2025

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
00:08

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

Published on: September 2, 2019

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周回性プロテアゼ-チャペロンDEGPの組み立て地における柔軟なクライアント依存のケージ

Robert W Harkness1,2,3,4, Zev A Ripstein1,2,3,4, Justin M Di Trani4

  • 1Department of Biochemistry, University of Toronto, Toronto M5S 1A8, Canada.

Journal of the American Chemical Society
|June 7, 2023
PubMed
まとめ

細菌のタンパク質DegPは ストレス中にクライアントタンパク質を捕捉し 処理するために 檻のような構造を形成します この研究は,DegPが

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Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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