Abstract
Oxidation of protein methionines to methionine sulfoxides can result in protein structural alterations with a wide variety of biological implications. Factors that determine susceptibility to oxidation are not well understood. The recent JBC Editors Pick by Walker et al. applied proteomic methodologies to show that the oxidative susceptibility of buried methionine residues is strongly correlated with folding stability of the contextual peptide. Proteome-wide analysis of oxidation-susceptible methionines promises to answer open questions about the biological functions of reversible methionine oxidation.