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Updated: May 20, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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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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原子解像度でのHSPB1チャペロンオリゴメアの構成異質性を捉える

Raymond F Berkeley1, Alexander P Plonski1, Tien M Phan2

  • 1Department of Chemistry and Biochemistry, University of California San Diego, La Jolla, California 92093, United States.

Journal of the American Chemical Society
|March 27, 2025
PubMed
まとめ

HSPB1のような小さな熱ショックタンパク質 (sHSP) は,細胞のプロテオスタシスと生物学的凝縮体を調節する. この研究はHSPB1を明らかにしています.

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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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