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JoVE Journal
Biochemistry

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
 

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Article DOI: 10.3791/57806-v 10:24 min June 7th, 2018
June 7th, 2018

Capitoli

Riepilogo

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.

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Keywords: Hsp33 Chaperone Activity Hydrogen-deuterium Exchange Mass Spectrometry Oxidative Stress Protein Aggregation Protein Dynamics Enzyme Interactions Visual Demonstration
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