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Updated: Aug 5, 2026

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

Multistep mechanism of substrate binding determines chaperone activity of Hsp70

M P Mayer1, H Schröder, S Rüdiger

  • 1Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Str.7, 79104 D-Freiburg, Germany.

Nature Structural Biology
|July 6, 2000
PubMed

Keywords:
Hsp70 functionProtein folding mechanismsDnaK substrate bindingATP-dependent chaperone activity

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