Radical-directed dissociation (RDD) is a method employing photodissociation to create an active radical at a site-specific location, which can subsequently be employed to cause fragmentation. The method is compatible with intact protein characterization, and RDD can be tuned to favor highly specific fragmentation channels or for the extraction of structural information. Protein structure can be mapped by initiating a radical at a single location, which leads to RDD at sites that are proximal in space following brief radical migration. Alternatively, fragmentation of the backbone at particular residues can be favored by creating the initial radical in a position primed to cleave the backbone, producing large fragments that can be subsequently sequenced. In this presentation, we will explore the factors that influence radical generation and site-specific cleavage within proteins including the nature of the chromophore and various activation parameters and strategies.

Radical-directed dissociation for top-down analysis of proteins

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