This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The basic reactivity of sulfur-centered radicals is being studied in a variety of peptide/protein systems using Sulfur K-edge X-ray Absorption Spectroscopy (S K-edge XAS) as a novel probe of the electronic structure of these biologically-important peptidic radicals. Cysteinyl radicals ([CysS?]), their sulfoxyl derivatives ([CysSOn]?) disulfide anion radicals ([CysS?SCys]1-) have been observed or postulated as intermediates in several biological functions including enzymatic catalysis, long-range electron transfer, peptide post-translational modification, cellular redox buffering, and even cellular redox signaling. Methionine radicals ([MetS?]) are believed to be involved in neurodegenerative diseases pathways such as the formation of amyloid-beta plaques. Electron paramagnetic resonance is the primary tool used for characterization of radical species but this approach is complicated by spin orbit broadening in sulfur species. The S 3p
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