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Significance Most natural proteins fold into a native folded conformation stabilized by noncovalent interactions. The free-energy difference between the folded and unfolded conformations of a protein (“thermodynamic folding stability”) establishes the fraction of its population that is in a folded conformation at equilibrium. Here, we used a mass spectrometry-based approach to measure the stabilities of ∼10,000 unique domains within ∼3,000 proteins in human cell extracts. Our data provide a global census of the magnitudes of folding stabilities within the human proteome and identify specific subsets of the proteome that are enriched in stable and unstable domains. We also show that the stability of proteins impacts their tendency to become oxidized and is globally altered by the chemical chaperone trimethylamineN -oxide (TMAO).

Global analysis of methionine oxidation provides a census of folding stabilities for the human proteome