Structural preferences of cysteine sulfinic acid: The sulfinate engages in multiple local interactions with the peptide backbone.

ABSTRACT: Cysteine sulfinic acid (Cys-SO₂^-) is a non-enzymatic oxidative post-translational modification (PTM) that has been identified in hundreds of proteins. However, the effects of cysteine sulfination are in most cases poorly understood. Cys-SO₂^- is structurally distinctive, with long sulfur-carbon and sulfur-oxygen bonds, and with tetrahedral geometry around sulfur due to its lone pair. Cys-SO₂^- thus has a unique range of potential interactions with the protein backbone which could facilitate protein structural changes. Herein, the structural effects of cysteine oxidation to the sulfinic acid were investigated in model peptides and folded proteins using NMR spectroscopy, circular dichroism, bioinformatics, and computational stud

SUBMITTER: Urmey AR 

PROVIDER: S-EPMC10204619 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature