Assessment of Protein Conformation via Diazirine-Promoted Oxidation of Methionine and Tryptophan Residues

, holo- and apo-myoglobin, and native and copper-bound β-2-microglobulin. In all surveyed protein systems but ubiquitin, this diazirine-promoted oxidation readily differentiates between the two protein conformations.

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Journal
Analytical Chemistry
Published
2026-05-12
DOI
https://doi.org/10.1021/acs.analchem.5c08256
Primary Topic
Redox biology and oxidative stress
Type
article
Field-Weighted Citation Impact
0.00

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article

Assessment of Protein Conformation via Diazirine-Promoted Oxidation of Methionine and Tryptophan Residues

Supadach Prertprawnon, Nicholas B. Borotto, Salem R. Neufeld
Analytical Chemistry
Redox biology and oxidative stress
article

Assessment of Protein Conformation via Diazirine-Promoted Oxidation of Methionine and Tryptophan Residues

Supadach Prertprawnon, Nicholas B. Borotto, Salem R. Neufeld
article en

Abstract

, holo- and apo-myoglobin, and native and copper-bound β-2-microglobulin. In all surveyed protein systems but ubiquitin, this diazirine-promoted oxidation readily differentiates between the two protein conformations.

Analytical Chemistry
University of Nevada, Reno (US)
National Institute of General Medical Sciences
Openalex Percentile: Top 8%
Redox biology and oxidative stress
DOIOpen Access PDFOpenAlex
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Assessment of Protein Conformation via Diazirine-Promoted Oxidation of Methionine and Tryptophan Residues — Supadach Prertprawnon, Nicholas B. Borotto, et al. · Analytical Chemistry (2026) | TGRS Research Map | TGRS