What question did this study set out to answer?

The research aims to evaluate how diazirine-promoted oxidation can distinguish between different protein conformations.

May 14, 2026Analytical Chemistry0 citationsOpen Access

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

SPSupadach PrertprawnonUniversity of Nevada, Reno SNSalem R. NeufeldUniversity of Nevada, Reno NBNicholas B. BorottoUniversity of Nevada, Reno

Key Points

The research aims to evaluate how diazirine-promoted oxidation can distinguish between different protein conformations.
Assessed holo- and apo-myoglobin alongside native and copper-bound β-2-microglobulin.
Applied diazirine-promoted oxidation to evaluate changes in protein structure.
Diazirine oxidation effectively differentiated protein conformations in all tested systems except ubiquitin.

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.

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