相关实验视频

Updated: Sep 9, 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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通过马尔科夫状态建模和NMR抑制辅助分子动力学模拟阐明Hsp70 Chaperone在客户端蛋白质折叠中的作用

Michael S O'Connor1, Kirill A Konovalov2, Josephine L Duvall2

  • 1Biophysics Graduate Program, University of Wisconsin-Madison, Madison, WI, 53706, USA.

Biophysical journal
|August 28, 2025
PubMed
概括

热冲击蛋白70 (Hsp70) 使用其闭盖状态来帮助像SH3这样的客户端蛋白正确折叠. 这种相互作用通过稳定特定的非极性残留物来防止错误折叠,揭示了伴侣辅助蛋白质折叠的关键机制.

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

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相关概念视频

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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Protein Folding

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Energy to Drive Translocation

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