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Updated: Aug 10, 2026

Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

タンパク質の記憶は,分子内チャペロンが媒介する変化した折りたたみによるものです

U P Shinde1, J J Liu, M Inouye

  • 1Department of Biochemistry, Robert Wood Johnson Medical School-UMDNJ, Piscataway, New Jersey 08854, USA.

Nature
|October 23, 1997
PubMed
まとめ

サブティリシンプロペプチドは,分子内チャペロンとして働き,プロテアゼドメインの折り畳みを誘導します. 付随者の突然変異により,超生命体が生成される.

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4D Imaging of Protein Aggregation in Live Cells08:59

4D Imaging of Protein Aggregation in Live Cells

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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

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Protein Folding01:22

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Protein Folding01:25

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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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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
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