Hsp33 protein is a
molecular chaperone
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assi ...
, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H
2O
2 cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.
References
{{InterPro content, IPR000397
Heat shock proteins
Molecular chaperones