AI Article Synopsis
- Hydroxyl radicals from synchrotron X-ray exposure create stable oxidative changes in amino acid side chains of proteins, revealing insights into protein structure.
- Following this, researchers use HPLC/MS analysis to measure how these side chains react and identify where the modifications occur through MS/MS analysis.
- The study highlights the method's application to the actin cytoskeleton, detailing specific binding sites and structural changes in actin and its interactions with proteins like gelsolin and cofilin.
Article Abstract
Hydroxyl radicals generated from millisecond exposure of aqueous solutions to synchrotron X-rays react with proteins to yield stable oxidative modifications of solvent-accessible amino acid side chains. Following proteolysis, HPLC/MS analysis is performed to quantitate the side chain reactivities, and MS/MS analysis is used to identify the modification site(s). Side chain reactivity is shown to be correlated with solvent accessibility; thus the method provides detailed site-specific information about protein structure. The application of these techniques to the study of the actin cytoskeleton is described in detail, including defining the binding sites of monomeric actin with gelsolin segment-1, the actin monomer binding surface on cofilin, the divalent cation-dependent structure changes of monomeric actin, and the conformational changes associated with actin filamentous assembly.
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