Comparative informatics analysis to evaluate site-specific protein oxidation in multidimensional LC-MS/MS data.

ABSTRACT: Redox proteomics has yielded molecular insight into diseases of protein dysfunction attributable to oxidative stress, underscoring the need for robust detection of protein oxidation products. Additionally, oxidative protein surface mapping techniques utilize hydroxyl radicals to gain structural insight about solvent exposure. Interpretation of tandem mass spectral data is a critical challenge for such investigations, because reactive oxygen species target a wide breadth of amino acids. Additionally, oxidized peptides may be generated in a wide range of abundances since the reactivity of hydroxyl radicals with different amino acids spans 3 orders of magnitude. Taken together, these attributes of oxidative footprinting pose both experimental and computational challenges to detecting oxidized

SUBMITTER: McClintock CS 

PROVIDER: S-EPMC3747030 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature