Mapping protein-protein interactions by localized oxidation: consequences of the reach of hydroxyl radical.

ABSTRACT: Hydroxyl radicals generated from a variety of methods, including not only synchrotron radiation but also Fenton reactions involving chelated iron, have become an accepted macromolecular footprinting tool. Hydroxyl radicals react with proteins via multiple mechanisms that lead to both polypeptide backbone cleavage events and side chain modifications (e.g., hydroxylation and carbonyl formation). The use of site-specifically tethered iron chelates can reveal protein-protein interactions, but the interpretation of such experiments will be strengthened by improving our understanding of how hydroxyl radicals produced at a point on a protein react with other protein sites. We have developed methods for monitoring carbonyl formation on proteins as a function of distance from a hydroxyl generator,

SUBMITTER: Cheal SM 

PROVIDER: S-EPMC2713361 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature