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Defining Hsp33’s Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Chapters
- 00:04Title
- 00:44Preparation of Fully Reduced and Fully Oxidized Proteins
- 02:37Light Scattering Aggregation Assay
- 05:20Hydrogen-deuterium Exchange Mass Spectrometry (HDX-MS)
- 08:01Results: Investigation of Hsp33 s Redox-regulated Chaperone Activity and Structure Changes
- 09:34Conclusion
One of the most challenging stress conditions that organisms encounter during their lifetime involves the accumulation of oxidants. During oxidative stress, cells heavily rely on molecular chaperones. Here, we present methods used to investigate the redox-regulated anti-aggregation activity, as well as to monitor structural changes governing the chaperone function using HDX-MS.
