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Updated: Aug 11, 2026

Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae
Published on: July 9, 2013
On the path to the heat shock response: destabilization and formation of partially folded protein intermediates, a
M L Freeman1, M J Borrelli, M J Meredith
1Department of Radiation Oncology, Vanderbilt Cancer Center, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Michael.Freeman@mcmail.vanderbilt.edu
Abstract:
This review discusses the initial events that occur during oxidative stress that induce the synthesis of heat shock proteins. The focus is on non-native oxidation or modification of protein thiols and the destablization that can result. Proteins that contain non-native modified thiols can become destablized such that they unfold into molten globule-like intermediates at or below 37 degrees C, relieving Hsf-1 negative regulation, and inducing Hsp transcription.
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