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Updated: Jul 9, 2026

Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes

Enabling Real-Time Compensation in Fast Photochemical Oxidations of Proteins for the Determination of Protein Topography Changes

Published on: September 1, 2020

Characterization of Oxidative Modifications to Short Peptides Using Low Dose Rate X-Rays.

Savannah Kidd¹, Thomas McCarthy¹, Simruthi Subramanian¹

¹Lawrence Berkeley National Laboratory, Molecular Foundry Division, Berkeley, CA 94720, USA.

Applied Sciences (Basel, Switzerland)

|July 8, 2026

Summary

This study demonstrates X-ray footprinting and mass spectrometry (XFMS) using low dose rate X-rays. The method characterizes oxidative peptide modifications and hydrogen peroxide production, offering insights into hydroxyl radical damage.

Keywords:

X-ray methods hydroxyl radical footprinting peptide oxidation

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Characterizing Cellular Proteins with In-cell Fast Photochemical Oxidation of Proteins

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Published on: March 11, 2020

Area of Science:

Structural Biology
Biophysical Chemistry
Mass Spectrometry

Background:

X-ray footprinting and mass spectrometry (XFMS) is an established technique in structural biology.
It relies on hydroxyl radicals produced by X-ray radiolysis to modify protein sidechains.
High flux synchrotron sources minimize scavenging and secondary reactions.

Purpose of the Study:

To demonstrate the feasibility of XFMS using low dose rate X-rays from a commercial instrument.
To characterize oxidative modifications on short peptides.
To quantify hydrogen peroxide production under low dose rate X-ray exposure.

Main Methods:

Application of X-ray footprinting and mass spectrometry (XFMS).
Utilized low dose rate X-rays from a commercial instrument.
Analyzed short peptides under aerobic and low oxygen conditions.

Main Results:

Successfully characterized oxidative modifications of +14, +16, and +32 Da on peptides.
Quantified hydrogen peroxide production at various doses.
Demonstrated feasibility of XFMS with a low dose rate X-ray source.

Conclusions:

XFMS is feasible using low dose rate X-rays for peptide analysis.
Provides fundamental data on hydroxyl radical-induced oxidative damage to peptides.
Opens possibilities for XFMS applications with accessible X-ray sources.