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doi: 10.22543/7674.61.p130136 48 GrypT.VanholderR.VaneechoutteM.GlorieuxG

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Cys (239) one of the six cysteinyl residues, is poorly accessible when Hsp 33 is active, and remains reduced despite H2O2 exposure, and does not therefore react with the sixth cysteinyl, Cys (141 ), which is highly reactive toward chemical modifications, demonstrating that other factors such as amino acid sequence, and other amino acid/peptidyl properties also are important in protein folding

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