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Updated: Aug 17, 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
Is the manganese stabilizing 33 kDa protein of photosystem II attaining a 'natively unfolded' or 'molten globule'
T Shutova1, K Irrgang, V V Klimov
1Max-Volmer-Institute for Biophysical Chemistry, Technical University Berlin, Strasse des 17. Juni 135, D-10623, Berlin, Germany.
Abstract:
This study compares the properties of the extrinsic 33 kDa subunit acting as 'manganese stabilizing protein' (MSP) of the water oxidizing complex with characteristic features of proteins that are known to attain a 'natively unfolded' or a 'molten globule' structure. The analysis leads to the conclusion that the MSP in solution is most likely a 'molten globule' with well defined compact regions of beta structure. The possible role of these structural peculiarities of MSP in solution for its function as important constituent of the WOC is discussed.
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