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Updated: Aug 19, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018
Protein folding assisted by chaperones
Júlio C Borges1, Carlos H I Ramos
1Centro de Biologia Molecular Estrutural, Laboratório Nacional de Luz Síncrotron, CP 6192, 13084-971, Campinas, SP, Brazil.
Abstract:
Molecular chaperones are one of the most important cell defense mechanisms against protein aggregation and misfolding. These specialized proteins bind non-native states of other proteins and assist them in reaching a correctly folded and functional conformation. Chaperones also participate in protein translocation by membranes, in the stabilization of unstable protein conformers and regulatory factors, in the delivery of substrates for proteolysis and in the recovery of proteins from aggregates.
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