関連する実験動画

Updated: Oct 9, 2025

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

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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Hsp90-p23-GRの構造は,Hsp90クライアント再構成メカニズムを明らかにする

Chari M Noddings1, Ray Yu-Ruei Wang1, Jill L Johnson2

  • 1Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA, USA.

Nature
|December 23, 2021
PubMed
まとめ

熱ショックタンパク質90 (Hsp90) とそのコチャペロンp23は,グルココルチコイド受容体 (GR) を本来のリガンド結合状態に再構成する. これはHsp90を明らかにします.

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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry11:37

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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