Protein folding stabilities are a major determinant of oxidation rates for buried methionine residues.

ABSTRACT: The oxidation of protein-bound methionines to form methionine sulfoxides has a broad range of biological ramifications, making it important to delineate factors that influence methionine oxidation rates within a given protein. This is especially important for biopharmaceuticals, where oxidation can lead to deactivation and degradation. Previously, neighboring residue effects and solvent accessibility have been shown to impact the susceptibility of methionine residues to oxidation. In this study, we provide proteome-wide evidence that oxidation rates of buried methionine residues are also strongly influenced by the thermodynamic folding stability of proteins. We surveyed the Escherichia coli proteome using several proteomic methodologies and globally measured oxidation rates of methionine r

SUBMITTER: Walker EJ 

PROVIDER: S-EPMC9062257 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature